Agarose-Bound – VectorLabs https://staging.vectorlabs.com From linker design and synthesis, bioconjugated design and manufacturing, biomolecule labeling and functionalization, and detection system and solutions, our team is here to help you move forward, with impact. Wed, 22 Oct 2025 17:02:15 +0000 en-US hourly 1 https://wordpress.org/?v=6.8.3 https://staging.vectorlabs.com/wp-content/uploads/2024/11/V-favicon-02-100x100.png Agarose-Bound – VectorLabs https://staging.vectorlabs.com 32 32 Galanthus Nivalis Lectin (GNL), Agarose bound https://staging.vectorlabs.com/products/agarose-bound-galanthus-nivalis-lectin-gnl/ Tue, 02 May 2023 04:46:53 +0000 https://staging.vectorlabs.com/?post_type=product&p=14020 Description

Agarose bound Galanthus nivalis lectin is prepared using our affinity-purified lectins. Galanthus nivalis lectin, unlike most mannose-specific lectins, is not a metalloprotein and does not require Ca++ or Mn++ for binding. Binding seems to be preferentially directed toward structures containing (α-1,3) mannose residues.

In contrast to most mannose-binding lectins, GNL will not bind α-linked glucose. Reports indicate that this lectin binds rat and mouse IgM but not IgG. The only protein from human serum reported to bind to this lectin is α2-macroglobulin. GNL binds to many viral glycoproteins.

Features:

  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Hydrophilic spacer arm is inserted between the lectin and the matrix
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer
  • 3 mg lectin/ml gel
  • Inhibiting/Eluting Sugar: 100 mM – 200 mM α-methylmannoside or Glycoprotein Eluting Solution (ES-1100)

Specifications

Unit Size 5 ml
Applications Glycobiology, Affinity Chromatography
Recommended Storage 2-8 °C DO NOT FREEZE
Solution 10 mM HEPES, pH 7.5, 0.15 M NaCl, 0.1 mM CaCl2, 0.01 mM MnCl2, 20 mM mannose, 0.08% sodium azide
Recommended Usage Wash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting Solution, Cat. No. ES-1100. Alternatively, 0.1 M α methyl mannoside can be used.For those glycoconjugates having a very high affinity for GNL, it may be necessary to lower the pH of the eluting sugar solution to pH 4.0 with acetic acid and increase the concentration of the α methyl mannoside to 0.5 M. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix Conjugate Lectins
Sugar Specificity Mannose
Conjugate Agarose

The post Galanthus Nivalis Lectin (GNL), Agarose bound appeared first on VectorLabs.

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Description

Agarose bound Galanthus nivalis lectin is prepared using our affinity-purified lectins. Galanthus nivalis lectin, unlike most mannose-specific lectins, is not a metalloprotein and does not require Ca++ or Mn++ for binding. Binding seems to be preferentially directed toward structures containing (α-1,3) mannose residues. 

In contrast to most mannose-binding lectins, GNL will not bind α-linked glucose. Reports indicate that this lectin binds rat and mouse IgM but not IgG. The only protein from human serum reported to bind to this lectin is α2-macroglobulin. GNL binds to many viral glycoproteins.

Features:

  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Hydrophilic spacer arm is inserted between the lectin and the matrix
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer
  • 3 mg lectin/ml gel
  • Inhibiting/Eluting Sugar: 100 mM – 200 mM α-methylmannoside or Glycoprotein Eluting Solution (ES-1100)

Specifications

Unit Size5 ml
ApplicationsGlycobiology, Affinity Chromatography
Recommended Storage2-8 °C DO NOT FREEZE
Solution10 mM HEPES, pH 7.5, 0.15 M NaCl, 0.1 mM CaCl2, 0.01 mM MnCl2, 20 mM mannose, 0.08% sodium azide
Recommended UsageWash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting Solution, Cat. No. ES-1100. Alternatively, 0.1 M α methyl mannoside can be used.For those glycoconjugates having a very high affinity for GNL, it may be necessary to lower the pH of the eluting sugar solution to pH 4.0 with acetic acid and increase the concentration of the α methyl mannoside to 0.5 M. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix ConjugateLectins
Sugar SpecificityMannose
ConjugateAgarose

Documents

Product FAQs

Our agarose lectin products are supplied as hydrated matrix solutions in amber glass bottles. The agarose (bead) material will settle and you will see two phases in the tube supplied. The upper phase is buffer. A column can be prepared in a commercial plastic device such as Bio-Rad Cat # 732-6008 or an inverted Pasteur pipet with glass wool lightly packed in the neck to retain the agarose. 1) Draw (pipet) the desired amount of settled agarose-lectin (gel) from the stock bottle into the prepared column and let the buffer drain by gravity.(Sometimes an air bubble in the column tip prevents flow; tapping the column should get the flow started). 2) Wash the gel with 10 column volumes of buffer, such as HBS (10 mM HEPES, 0.15 M NaCl, pH 7.5) and discard the flow through. 3) Place a collection vessel (e.g. glass test tube) under the column tip and apply the glycoprotein-containing solution.Allow the solution to drain through using gravity. We recommend against pushing or pulling the material through the column. Retain the flow through material until the desired binding has been confirmed. 4) After sample application, wash column with 2-3 column volumes of buffer (or until the absorbance at 280nm is reduced to a satisfactory level) to remove unbound materials before elution. 5) Place a fresh collection vessel under the column tip.Apply the eluting solution again letting gravity do the work of moving the solution over the column. Note that in some cases, several column volumes of eluting solution may be required to achieved adequate release of bound material. 6) Following elution, the column can be prepared for reuse by washing with 10 column volumes of buffer. 7) If the column is to be stored, equilibrate the column with buffer containing 0.08% sodium azide. Cover the column with a plastic wrap, or similar, to prevent desiccation and keep at 4 degrees Celsius. The column will be stable for many months when stored under these conditions.

The pH should be near neutral, the maximum pressure for packing the resin is 10 psi, and the maximum flow rate 3.5 ml/min.

Citations

Technical Information

Our coupling method provides several advantages over the traditional cyanogen bromide procedure:

  • Maximum carbohydrate binding activity of the coupled lectins is retained
  • Linkage is stable over a range of pH values
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges are present after conjugation. This minimizes non-specific binding to the matrix

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

Inhibiting/Eluting Sugar: 100 mM – 200 mM α-methylmannoside

The post Galanthus Nivalis Lectin (GNL), Agarose bound appeared first on VectorLabs.

]]> Jacalin, Agarose bound https://staging.vectorlabs.com/products/jacalin-agarose-bound/ Tue, 02 May 2023 04:42:09 +0000 https://staging.vectorlabs.com/?post_type=product&p=14009 Description

Agarose bound Jacalin is prepared using our affinity-purified lectins. Jacalin is a lectin composed of four subunits of approximately 16 kDa each. This lectin appears to bind only O-glycosidically linked oligosaccharides, preferring the structure galactosyl (β-1,3) N-acetylgalactosamine. This structure (the T-antigen) is the oligosaccharide to which peanut agglutinin (PNA) binds. However, unlike PNA, Jacalin will bind a mono- or desialylated form of this structure. This lectin has been used to purify human IgA. The specificity of this lectin also affords the opportunity to localize or isolate glycoproteins with O-glycosidically linked oligosaccharide side chains.

Features:

  • Matrix is heat stable, cross-linked 4% agarose beads with a molecular exlusion of about 2×107 daltons
  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Product supplied as a 1:1 suspension in buffer

Specifications

Unit Size 10 ml
Applications Glycobiology, Affinity Chromatography
Recommended Storage 2-8 °C DO NOT FREEZE
Solution 10 mM HEPES, pH 7.5, 0.15 M NaCl, 0.1 mM CaCl2, 20 mM galactose, 20 mM lactose, 0.08% sodium azide
Recommended Usage Wash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Note:To optimize elution of glycoproteins, wash the gel with 10 column volumes of 175 mM TRIS, pH 7.5, before use.Glycoproteins should be applied in this buffer. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting Solution, Cat. No. ES-2100. Alternatively, 0.1 M melibiose or 0.8 M galactose in 175 mM TRIS, pH 7.5 can be used.Use of other buffers may result in a reduction in yield of eluted glycoproteins. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix Conjugate Lectins
Sugar Specificity Galactose
Conjugate Agarose

The post Jacalin, Agarose bound appeared first on VectorLabs.

]]>

Description

Agarose bound Jacalin is prepared using our affinity-purified lectins. Jacalin is a lectin composed of four subunits of approximately 16 kDa each. This lectin appears to bind only O-glycosidically linked oligosaccharides, preferring the structure galactosyl (β-1,3) N-acetylgalactosamine. This structure (the T-antigen) is the oligosaccharide to which peanut agglutinin (PNA) binds. However, unlike PNA, Jacalin will bind a mono- or desialylated form of this structure. This lectin has been used to purify human IgA. The specificity of this lectin also affords the opportunity to localize or isolate glycoproteins with O-glycosidically linked oligosaccharide side chains.

Features:

  • Matrix is heat stable, cross-linked 4% agarose beads with a molecular exlusion of about 2×107 daltons
  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Product supplied as a 1:1 suspension in buffer

Specifications

Unit Size10 ml
ApplicationsGlycobiology, Affinity Chromatography
Recommended Storage2-8 °C DO NOT FREEZE
Solution10 mM HEPES, pH 7.5, 0.15 M NaCl, 0.1 mM CaCl2, 20 mM galactose, 20 mM lactose, 0.08% sodium azide
Recommended UsageWash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Note:To optimize elution of glycoproteins, wash the gel with 10 column volumes of 175 mM TRIS, pH 7.5, before use.Glycoproteins should be applied in this buffer. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting Solution, Cat. No. ES-2100. Alternatively, 0.1 M melibiose or 0.8 M galactose in 175 mM TRIS, pH 7.5 can be used.Use of other buffers may result in a reduction in yield of eluted glycoproteins. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix ConjugateLectins
Sugar SpecificityGalactose
ConjugateAgarose

Documents

Product FAQs

Our agarose lectin products are supplied as hydrated matrix solutions in amber glass bottles. The agarose (bead) material will settle and you will see two phases in the tube supplied. The upper phase is buffer. A column can be prepared in a commercial plastic device such as Bio-Rad Cat # 732-6008 or an inverted Pasteur pipet with glass wool lightly packed in the neck to retain the agarose. 1) Draw (pipet) the desired amount of settled agarose-lectin (gel) from the stock bottle into the prepared column and let the buffer drain by gravity.(Sometimes an air bubble in the column tip prevents flow; tapping the column should get the flow started). 2) Wash the gel with 10 column volumes of buffer, such as HBS (10 mM HEPES, 0.15 M NaCl, pH 7.5) and discard the flow through. 3) Place a collection vessel (e.g. glass test tube) under the column tip and apply the glycoprotein-containing solution.Allow the solution to drain through using gravity. We recommend against pushing or pulling the material through the column. Retain the flow through material until the desired binding has been confirmed. 4) After sample application, wash column with 2-3 column volumes of buffer (or until the absorbance at 280nm is reduced to a satisfactory level) to remove unbound materials before elution. 5) Place a fresh collection vessel under the column tip.Apply the eluting solution again letting gravity do the work of moving the solution over the column. Note that in some cases, several column volumes of eluting solution may be required to achieved adequate release of bound material. 6) Following elution, the column can be prepared for reuse by washing with 10 column volumes of buffer. 7) If the column is to be stored, equilibrate the column with buffer containing 0.08% sodium azide. Cover the column with a plastic wrap, or similar, to prevent desiccation and keep at 4 degrees Celsius. The column will be stable for many months when stored under these conditions.

The pH should be near neutral, the maximum pressure for packing the resin is 10 psi, and the maximum flow rate 3.5 ml/min.

Citations

Technical Information

Agarose bound* Jacalin is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2×107 daltons are used as the solid-phase matrix to which the lectins are covalently coupled. The attachment of the lectins to the beads is carefully controlled to preserve lectin activity and minimize conformational changes of the bound lectins that might result in nonspecific ionic or hydrophobic interactions. The technique we have developed to couple lectins to agarose beads inserts a hydrophilic spacer arm between the lectin and the matrix.

This coupling method provides several advantages over the traditional cyanogen bromide procedure:

  • Maximum carbohydrate binding activity of the coupled lectins is retained
  • Linkage is stable over a range of pH values
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges are present after conjugation. This minimizes non-specific binding to the matrix

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

Inhibiting/Eluting Sugar: 800 mM galactose or 100 mM melibiose or Glycoprotein Eluting Solution (ES-2100)

*4 mg lectin/ml gel

The post Jacalin, Agarose bound appeared first on VectorLabs.

]]> Ricinus Communis Agglutinin I (RCA I, RCA120), Agarose bound https://staging.vectorlabs.com/products/agarose-ricinus-communis-agglutinin/ Tue, 02 May 2023 04:37:34 +0000 https://staging.vectorlabs.com/?post_type=product&p=13999 Description

Agarose bound Ricinus communis agglutinin I is prepared using our affinity-purified lectins. This lectin consists of two subunits of 60 kDa which can be dissociated by reducing agents into closely related chains between 27 kDa and 33 kDa. One of the chains appears to be common to the B chain of another castor bean lectin, ricin, while the other chain is unique to RCA I.

Features:

  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer
  • Inhibiting/Eluting Sugar: 200 mM galactose or lactose or Glycoprotein Eluting Solution (ES-2100)

Specifications

Unit Size 5 ml
Applications Glycobiology, Affinity Chromatography
Recommended Storage 2-8 °C DO NOT FREEZE
Solution 10 mM HEPES, pH 7.5, 0.15 M NaCl, 20 mM lactose, 0.08% sodium azide
Recommended Usage Wash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting Solution, Cat. No. ES-2100. Alternatively, 200 mM galactose or lactose can be used. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix Conjugate Lectins
Sugar Specificity Galactose, Lactose
Conjugate Agarose

The post Ricinus Communis Agglutinin I (RCA I, RCA120), Agarose bound appeared first on VectorLabs.

]]>

Description

Agarose bound Ricinus communis agglutinin I is prepared using our affinity-purified lectins. This lectin consists of two subunits of 60 kDa which can be dissociated by reducing agents into closely related chains between 27 kDa and 33 kDa. One of the chains appears to be common to the B chain of another castor bean lectin, ricin, while the other chain is unique to RCA I.

Features:

  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer
  • Inhibiting/Eluting Sugar: 200 mM galactose or lactose or Glycoprotein Eluting Solution (ES-2100)

Specifications

Unit Size5 ml
ApplicationsGlycobiology, Affinity Chromatography
Recommended Storage2-8 °C DO NOT FREEZE
Solution10 mM HEPES, pH 7.5, 0.15 M NaCl, 20 mM lactose, 0.08% sodium azide
Recommended UsageWash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting Solution, Cat. No. ES-2100. Alternatively, 200 mM galactose or lactose can be used. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix ConjugateLectins
Sugar SpecificityGalactose, Lactose
ConjugateAgarose

Documents

Product FAQs

Our agarose lectin products are supplied as hydrated matrix solutions in amber glass bottles. The agarose (bead) material will settle and you will see two phases in the tube supplied. The upper phase is buffer. A column can be prepared in a commercial plastic device such as Bio-Rad Cat # 732-6008 or an inverted Pasteur pipet with glass wool lightly packed in the neck to retain the agarose. 1) Draw (pipet) the desired amount of settled agarose-lectin (gel) from the stock bottle into the prepared column and let the buffer drain by gravity.(Sometimes an air bubble in the column tip prevents flow; tapping the column should get the flow started). 2) Wash the gel with 10 column volumes of buffer, such as HBS (10 mM HEPES, 0.15 M NaCl, pH 7.5) and discard the flow through. 3) Place a collection vessel (e.g. glass test tube) under the column tip and apply the glycoprotein-containing solution.Allow the solution to drain through using gravity. We recommend against pushing or pulling the material through the column. Retain the flow through material until the desired binding has been confirmed. 4) After sample application, wash column with 2-3 column volumes of buffer (or until the absorbance at 280nm is reduced to a satisfactory level) to remove unbound materials before elution. 5) Place a fresh collection vessel under the column tip.Apply the eluting solution again letting gravity do the work of moving the solution over the column. Note that in some cases, several column volumes of eluting solution may be required to achieved adequate release of bound material. 6) Following elution, the column can be prepared for reuse by washing with 10 column volumes of buffer. 7) If the column is to be stored, equilibrate the column with buffer containing 0.08% sodium azide. Cover the column with a plastic wrap, or similar, to prevent desiccation and keep at 4 degrees Celsius. The column will be stable for many months when stored under these conditions.

The pH should be near neutral, the maximum pressure for packing the resin is 10 psi, and the maximum flow rate 3.5 ml/min.

Technical Information

Agarose bound* Ricinus communis agglutinin I is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2×107 daltons are used as the solid-phase matrix to which the lectins are covalently coupled. The attachment of the lectins to the beads is carefully controlled to preserve lectin activity and minimize conformational changes of the bound lectins that might result in nonspecific ionic or hydrophobic interactions. The technique we have developed to couple lectins to agarose beads inserts a hydrophilic spacer arm between the lectin and the matrix.

This coupling method provides several advantages over the traditional cyanogen bromide procedure:

  • Maximum carbohydrate binding activity of the coupled lectins is retained
  • Linkage is stable over a range of pH values

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

*4 mg lectin/ml gel

The post Ricinus Communis Agglutinin I (RCA I, RCA120), Agarose bound appeared first on VectorLabs.

]]> Peanut Agglutinin (PNA), Agarose bound https://staging.vectorlabs.com/products/agarose-bound-peanut-agglutinin/ Tue, 02 May 2023 04:31:26 +0000 https://staging.vectorlabs.com/?post_type=product&p=13987 Description

Agarose bound PNA is prepared using our affinity-purified lectins. Peanut agglutinin binds preferentially to the T-antigen, a galactosyl (β-1,3) N-acetylgalactosamine structure present in many glycoconjugates such as M and N blood groups, gangliosides, and many other soluble and membrane-associated glycoproteins and glycolipids. With certain exceptions, the receptor sequence for PNA is normally sialylated which prevents the lectin from binding to its receptor oligosaccharide (see Jacalin). Even sialic acid which is not bound directly to the receptor sugars may inhibit binding. The presence of calcium ions in diluents can enhance the binding of PNA to receptors, possibly by neutralizing the negative charges on sialic acid residues adjacent to the receptor sequence.

Features:

  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer
  • Inhibiting/Eluting Sugar: 200 mM galactose or Glycoprotein Eluting Solution (ES-2100)

Specifications

Unit Size 2 ml, 5 ml
Applications Glycobiology, Affinity Chromatography
Recommended Storage 2-8 °C DO NOT FREEZE
Solution 10 mM HEPES, pH 7.5, 0.15 M NaCl, 0.1 mM CaCl2, 20 mM galactose, 0.08% sodium azide
Recommended Usage Wash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Use of buffers containing 0.1 mM CaCl2 and 0.01 mM MnCl2 is recommended. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting Solution, Cat. No. ES-2100. Alternatively, 200 mM galactose in 10 mM HEPES-buffered saline, pH 7.5 can be used.For those glycoconjugates having very high affinity for PNA, it may be necessary to lower the pH of the eluting sugar solution to pH 3.0 with acetic acid. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix Conjugate Lectins
Sugar Specificity Galactose
Conjugate Agarose

The post Peanut Agglutinin (PNA), Agarose bound appeared first on VectorLabs.

]]>

Description

Agarose bound PNA is prepared using our affinity-purified lectins. Peanut agglutinin binds preferentially to the T-antigen, a galactosyl (β-1,3) N-acetylgalactosamine structure present in many glycoconjugates such as M and N blood groups, gangliosides, and many other soluble and membrane-associated glycoproteins and glycolipids. With certain exceptions, the receptor sequence for PNA is normally sialylated which prevents the lectin from binding to its receptor oligosaccharide (see Jacalin). Even sialic acid which is not bound directly to the receptor sugars may inhibit binding. The presence of calcium ions in diluents can enhance the binding of PNA to receptors, possibly by neutralizing the negative charges on sialic acid residues adjacent to the receptor sequence.

Features:

  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer
  • Inhibiting/Eluting Sugar: 200 mM galactose or Glycoprotein Eluting Solution (ES-2100)

Specifications

Unit Size2 ml, 5 ml
ApplicationsGlycobiology, Affinity Chromatography
Recommended Storage2-8 °C DO NOT FREEZE
Solution10 mM HEPES, pH 7.5, 0.15 M NaCl, 0.1 mM CaCl2, 20 mM galactose, 0.08% sodium azide
Recommended UsageWash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Use of buffers containing 0.1 mM CaCl2 and 0.01 mM MnCl2 is recommended. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting Solution, Cat. No. ES-2100. Alternatively, 200 mM galactose in 10 mM HEPES-buffered saline, pH 7.5 can be used.For those glycoconjugates having very high affinity for PNA, it may be necessary to lower the pH of the eluting sugar solution to pH 3.0 with acetic acid. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix ConjugateLectins
Sugar SpecificityGalactose
ConjugateAgarose

Documents

Product FAQs

Our agarose lectin products are supplied as hydrated matrix solutions in amber glass bottles. The agarose (bead) material will settle and you will see two phases in the tube supplied. The upper phase is buffer. A column can be prepared in a commercial plastic device such as Bio-Rad Cat # 732-6008 or an inverted Pasteur pipet with glass wool lightly packed in the neck to retain the agarose. 1) Draw (pipet) the desired amount of settled agarose-lectin (gel) from the stock bottle into the prepared column and let the buffer drain by gravity.(Sometimes an air bubble in the column tip prevents flow; tapping the column should get the flow started). 2) Wash the gel with 10 column volumes of buffer, such as HBS (10 mM HEPES, 0.15 M NaCl, pH 7.5) and discard the flow through. 3) Place a collection vessel (e.g. glass test tube) under the column tip and apply the glycoprotein-containing solution.Allow the solution to drain through using gravity. We recommend against pushing or pulling the material through the column. Retain the flow through material until the desired binding has been confirmed. 4) After sample application, wash column with 2-3 column volumes of buffer (or until the absorbance at 280nm is reduced to a satisfactory level) to remove unbound materials before elution. 5) Place a fresh collection vessel under the column tip.Apply the eluting solution again letting gravity do the work of moving the solution over the column. Note that in some cases, several column volumes of eluting solution may be required to achieved adequate release of bound material. 6) Following elution, the column can be prepared for reuse by washing with 10 column volumes of buffer. 7) If the column is to be stored, equilibrate the column with buffer containing 0.08% sodium azide. Cover the column with a plastic wrap, or similar, to prevent desiccation and keep at 4 degrees Celsius. The column will be stable for many months when stored under these conditions.

The pH should be near neutral, the maximum pressure for packing the resin is 10 psi, and the maximum flow rate 3.5 ml/min.

Citations

Technical Information

PNA is useful in distinguishing between normal and tumor tissues and in assessing malignancy in transitional mucosa. In addition, PNA binding can be used to measure cellular maturity in lymphoid tissues, to distinguish a variety of lymphocyte subpopulations in man and experimental animals, and to measure the levels of lymphoid cell populations in many diseases. PNA can be employed in the fractionation of stem cells in mice for use in bone marrow transplantation across histocompatibility barriers.

A major cell surface receptor for PNA may be asialo GM1 ganglioside. Since PNA shares specificity with the antibody to this glycolipid, PNA and the antibody can be used interchangeably in some applications.

Agarose bound* PNA is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2×107 daltons are used as the solid-phase matrix to which the lectins are covalently coupled. The attachment of the lectins to the beads is carefully controlled to preserve lectin activity and minimize conformational changes of the bound lectins that might result in nonspecific ionic or hydrophobic interactions. The technique we have developed to couple lectins to agarose beads inserts a hydrophilic spacer arm between the lectin and the matrix.

This coupling method provides several advantages over the traditional cyanogen bromide procedure:

  • Maximum carbohydrate binding activity of the coupled lectins is retained
  • Linkage is stable over a range of pH values

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

*5 mg lectin/ml gel

The post Peanut Agglutinin (PNA), Agarose bound appeared first on VectorLabs.

]]> Succinylated Wheat Germ Agglutinin (WGA), Agarose bound https://staging.vectorlabs.com/products/succinylated-wheat-germ-agglutinin-wga-agarose-bound/ Tue, 02 May 2023 04:25:10 +0000 https://staging.vectorlabs.com/?post_type=product&p=13977 Description

Agarose bound, succinylated WGA is prepared using our affinity-purified lectins. This derivative has been reported to have properties distinct from the native lectin. Evidence suggests that Succinylated Wheat Germ agglutinin does not bind to sialic acid residues, unlike the native form, but retains its specificity toward N-acetylglucosamine. Using conjugates of the native lectin and the succinylated form can provide a system to distinguish between sialylated glycoconjugates and those containing only N-acetylglucosamine structures.

Features:

  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Product supplied as a 1:1 suspension in buffer
  • Inhibiting/Eluting Sugar: Chitin Hydrolysate; or 500 mM N-acetylglucosamine with salt and/or acid elution generally required; or Glycoprotein Eluting Solution (ES-5100)

Specifications

Unit Size 2 ml
Applications Glycobiology, Affinity Chromatography
Recommended Storage 2-8 °C DO NOT FREEZE
Solution 10 mM HEPES, pH 7.5, 0.15 M NaCl, 20 mM GlcNAc, 0.08% sodium azide
Recommended Usage Wash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting solution, Cat. No. ES-5100. Alternatively, 0.5 M N-Acetyl-D-Glucosamine (GlcNAc) can be used.For those glycoconjugates having very high affinity for WGA, it may be necessary to lower the pH of the eluting sugar solution to pH 3.0 with acetic acid and increase the concentration of GlcNAc. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix Conjugate Lectins
Sugar Specificity N-Acetylglucosamine
Conjugate Agarose

The post Succinylated Wheat Germ Agglutinin (WGA), Agarose bound appeared first on VectorLabs.

]]>

Description

Agarose bound, succinylated WGA is prepared using our affinity-purified lectins. This derivative has been reported to have properties distinct from the native lectin. Evidence suggests that Succinylated Wheat Germ agglutinin does not bind to sialic acid residues, unlike the native form, but retains its specificity toward N-acetylglucosamine. Using conjugates of the native lectin and the succinylated form can provide a system to distinguish between sialylated glycoconjugates and those containing only N-acetylglucosamine structures.

Features:

  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Product supplied as a 1:1 suspension in buffer
  • Inhibiting/Eluting Sugar: Chitin Hydrolysate; or 500 mM N-acetylglucosamine with salt and/or acid elution generally required; or Glycoprotein Eluting Solution (ES-5100)

Specifications

Unit Size2 ml
ApplicationsGlycobiology, Affinity Chromatography
Recommended Storage2-8 °C DO NOT FREEZE
Solution10 mM HEPES, pH 7.5, 0.15 M NaCl, 20 mM GlcNAc, 0.08% sodium azide
Recommended UsageWash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting solution, Cat. No. ES-5100. Alternatively, 0.5 M N-Acetyl-D-Glucosamine (GlcNAc) can be used.For those glycoconjugates having very high affinity for WGA, it may be necessary to lower the pH of the eluting sugar solution to pH 3.0 with acetic acid and increase the concentration of GlcNAc. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix ConjugateLectins
Sugar SpecificityN-Acetylglucosamine
ConjugateAgarose

Documents

Product FAQs

Our agarose lectin products are supplied as hydrated matrix solutions in amber glass bottles. The agarose (bead) material will settle and you will see two phases in the tube supplied. The upper phase is buffer. A column can be prepared in a commercial plastic device such as Bio-Rad Cat # 732-6008 or an inverted Pasteur pipet with glass wool lightly packed in the neck to retain the agarose. 1) Draw (pipet) the desired amount of settled agarose-lectin (gel) from the stock bottle into the prepared column and let the buffer drain by gravity.(Sometimes an air bubble in the column tip prevents flow; tapping the column should get the flow started). 2) Wash the gel with 10 column volumes of buffer, such as HBS (10 mM HEPES, 0.15 M NaCl, pH 7.5) and discard the flow through. 3) Place a collection vessel (e.g. glass test tube) under the column tip and apply the glycoprotein-containing solution.Allow the solution to drain through using gravity. We recommend against pushing or pulling the material through the column. Retain the flow through material until the desired binding has been confirmed. 4) After sample application, wash column with 2-3 column volumes of buffer (or until the absorbance at 280nm is reduced to a satisfactory level) to remove unbound materials before elution. 5) Place a fresh collection vessel under the column tip.Apply the eluting solution again letting gravity do the work of moving the solution over the column. Note that in some cases, several column volumes of eluting solution may be required to achieved adequate release of bound material. 6) Following elution, the column can be prepared for reuse by washing with 10 column volumes of buffer. 7) If the column is to be stored, equilibrate the column with buffer containing 0.08% sodium azide. Cover the column with a plastic wrap, or similar, to prevent desiccation and keep at 4 degrees Celsius. The column will be stable for many months when stored under these conditions.

The pH should be near neutral, the maximum pressure for packing the resin is 10 psi, and the maximum flow rate 3.5 ml/min.

Citations

Technical Information

Agarose bound*, succinylated WGA is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2×107 daltons are used as the solid-phase matrix to which the lectins are covalently coupled. The attachment of the lectins to the beads is carefully controlled to preserve lectin activity and minimize conformational changes of the bound lectins that might result in nonspecific ionic or hydrophobic interactions. The technique we have developed to couple lectins to agarose beads inserts a hydrophilic spacer arm between the lectin and the matrix.

This coupling method provides several advantages over the traditional cyanogen bromide procedure:

  • Maximum carbohydrate binding activity of the coupled lectins is retained
  • Linkage is stable over a range of pH values
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges are present after conjugation. This minimizes non-specific binding to the matrix

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

*1 mg lectin/ml gel

The post Succinylated Wheat Germ Agglutinin (WGA), Agarose bound appeared first on VectorLabs.

]]> Wheat Germ Agglutinin (WGA), Agarose bound https://staging.vectorlabs.com/products/agarose-bound-wheat-germ-agglutinin/ Tue, 02 May 2023 02:49:47 +0000 https://staging.vectorlabs.com/?post_type=product&p=13963 Description

Agarose bound Wheat germ agglutinin (WGA) is prepared using 4% agarose beads. The receptor sugar for WGA is N-acetylglucosamine, with preferential binding to dimers and trimers of this sugar. WGA can bind oligosaccharides containing terminal N-acetylglucosamine or chitobiose, structures which are common to many serum and membrane glycoproteins.

Features:

  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer

Specifications

Unit Size 2 ml, 10 ml
Applications Glycobiology, Affinity Chromatography
Recommended Storage 2-8 °C DO NOT FREEZE
Solution 10 mM HEPES, pH 7.5, 0.15 M NaCl, 20 mM GlcNAc, 0.08% sodium azide
Recommended Usage Wash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting solution, Cat. No. ES-5100. Alternately, 0.5 M N-Acetyl-D-Glucosamine or Chitin Hydrolysate (Cat. No. SP-0090) can be used. For those glycoconjugates having very high affinity for WGA, it may be necessary to lower the pH of the eluting sugar solution to pH 3.0 with acetic acid. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix Conjugate Lectins
Sugar Specificity N-Acetylglucosamine
Conjugate Agarose

The post Wheat Germ Agglutinin (WGA), Agarose bound appeared first on VectorLabs.

]]>

Description

Agarose bound Wheat germ agglutinin (WGA) is prepared using 4% agarose beads. The receptor sugar for WGA is N-acetylglucosamine, with preferential binding to dimers and trimers of this sugar. WGA can bind oligosaccharides containing terminal N-acetylglucosamine or chitobiose, structures which are common to many serum and membrane glycoproteins. 

Features:

  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer

Specifications

Unit Size2 ml, 10 ml
ApplicationsGlycobiology, Affinity Chromatography
Recommended Storage2-8 °C DO NOT FREEZE
Solution10 mM HEPES, pH 7.5, 0.15 M NaCl, 20 mM GlcNAc, 0.08% sodium azide
Recommended UsageWash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting solution, Cat. No. ES-5100. Alternately, 0.5 M N-Acetyl-D-Glucosamine or Chitin Hydrolysate (Cat. No. SP-0090) can be used. For those glycoconjugates having very high affinity for WGA, it may be necessary to lower the pH of the eluting sugar solution to pH 3.0 with acetic acid. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix ConjugateLectins
Sugar SpecificityN-Acetylglucosamine
ConjugateAgarose

Documents

Product FAQs

Our agarose lectin products are supplied as hydrated matrix solutions in amber glass bottles. The agarose (bead) material will settle and you will see two phases in the tube supplied. The upper phase is buffer. A column can be prepared in a commercial plastic device such as Bio-Rad Cat # 732-6008 or an inverted Pasteur pipet with glass wool lightly packed in the neck to retain the agarose. 1) Draw (pipet) the desired amount of settled agarose-lectin (gel) from the stock bottle into the prepared column and let the buffer drain by gravity.(Sometimes an air bubble in the column tip prevents flow; tapping the column should get the flow started). 2) Wash the gel with 10 column volumes of buffer, such as HBS (10 mM HEPES, 0.15 M NaCl, pH 7.5) and discard the flow through. 3) Place a collection vessel (e.g. glass test tube) under the column tip and apply the glycoprotein-containing solution.Allow the solution to drain through using gravity. We recommend against pushing or pulling the material through the column. Retain the flow through material until the desired binding has been confirmed. 4) After sample application, wash column with 2-3 column volumes of buffer (or until the absorbance at 280nm is reduced to a satisfactory level) to remove unbound materials before elution. 5) Place a fresh collection vessel under the column tip.Apply the eluting solution again letting gravity do the work of moving the solution over the column. Note that in some cases, several column volumes of eluting solution may be required to achieved adequate release of bound material. 6) Following elution, the column can be prepared for reuse by washing with 10 column volumes of buffer. 7) If the column is to be stored, equilibrate the column with buffer containing 0.08% sodium azide. Cover the column with a plastic wrap, or similar, to prevent desiccation and keep at 4 degrees Celsius. The column will be stable for many months when stored under these conditions.

The pH should be near neutral, the maximum pressure for packing the resin is 10 psi, and the maximum flow rate 3.5 ml/min.

Citations

Technical Information

Bacterial cell wall peptidoglycans, chitin, cartilage glycosaminoglycans, and glycolipids can also bind WGA. Native WGA has also been reported to interact with some glycoproteins via sialic acid residues (see succinylated WGA). This lectin is used for the purification of insulin receptors and for neuronal tracing.

Agarose bound* WGA is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2×107 daltons are used as the solid-phase matrix to which the lectins are covalently coupled. The attachment of the lectins to the beads is carefully controlled to preserve lectin activity and minimize conformational changes of the bound lectins that might result in nonspecific ionic or hydrophobic interactions. The technique we have developed to couple lectins to agarose beads inserts a hydrophilic spacer arm between the lectin and the matrix.

This coupling method provides several advantages over the traditional cyanogen bromide procedure:

  • Maximum carbohydrate binding activity of the coupled lectins is retained
  • Linkage is stable over a range of pH values
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges are present after conjugation. This minimizes non-specific binding to the matrix.

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

Inhibiting/Eluting Sugar: Chitin Hydrolysate or 500 mM N-acetylglucosamine with salt and/or acid elution generally required

*5 mg lectin/ml gel

The post Wheat Germ Agglutinin (WGA), Agarose bound appeared first on VectorLabs.

]]> Concanavalin A (Con A), Agarose bound https://staging.vectorlabs.com/products/agarose-bound-concanavalin-a-con-a/ Tue, 02 May 2023 02:40:58 +0000 https://staging.vectorlabs.com/?post_type=product&p=13951

Description

Agarose bound Con A is prepared using our affinity-purified lectins. Con A recognizes α-linked mannose present as part of a core oligosaccharide in many serum and membrane glycoproteins. At neutral and alkaline pH, Con A exists as a tetramer of four identical subunits; below pH 5.6, Con A dissociates into active dimers of 52 kDa. Acetylation, succinylation, or other derivatizations can also produce stable forms with dimeric structures. (See succinylated Con A). Nicks in the sequence are often present in the purest preparations due to hydrolytic damage within the seeds.

Features:

  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Hydrophilic spacer arm is inserted between the lectin and the matrix
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer

Specifications

Unit Size 10 ml, 100 ml
Applications Glycobiology, Affinity Chromatography
Recommended Storage 2-8 °C DO NOT FREEZE
Solution 10 mM HEPES, pH 7.5, 0.15 M NaCl, 0.1 mM CaCl2, 0.01 mM MnCl2, 20 mM glucose, 0.08% sodium azide
Recommended Usage Wash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting Solution, Cat. No. ES-1100. Alternatively, a 0.2 M α-methyl mannoside/0.2 M α-methyl glucoside mixture can be used. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix Conjugate Lectins
Sugar Specificity Mannose, Glucose
Conjugate Agarose

The post Concanavalin A (Con A), Agarose bound appeared first on VectorLabs.

]]>

Description

Agarose bound Con A is prepared using our affinity-purified lectins. Con A recognizes α-linked mannose present as part of a core oligosaccharide in many serum and membrane glycoproteins. At neutral and alkaline pH, Con A exists as a tetramer of four identical subunits; below pH 5.6, Con A dissociates into active dimers of 52 kDa. Acetylation, succinylation, or other derivatizations can also produce stable forms with dimeric structures. (See succinylated Con A). Nicks in the sequence are often present in the purest preparations due to hydrolytic damage within the seeds.

Features:

  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Hydrophilic spacer arm is inserted between the lectin and the matrix
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer

Specifications

Unit Size10 ml, 100 ml
ApplicationsGlycobiology, Affinity Chromatography
Recommended Storage2-8 °C DO NOT FREEZE
Solution10 mM HEPES, pH 7.5, 0.15 M NaCl, 0.1 mM CaCl2, 0.01 mM MnCl2, 20 mM glucose, 0.08% sodium azide
Recommended UsageWash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting Solution, Cat. No. ES-1100. Alternatively, a 0.2 M α-methyl mannoside/0.2 M α-methyl glucoside mixture can be used. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix ConjugateLectins
Sugar SpecificityMannose, Glucose
ConjugateAgarose

Documents

Product FAQs

Our agarose lectin products are supplied as hydrated matrix solutions in amber glass bottles. The agarose (bead) material will settle and you will see two phases in the tube supplied. The upper phase is buffer. A column can be prepared in a commercial plastic device such as Bio-Rad Cat # 732-6008 or an inverted Pasteur pipet with glass wool lightly packed in the neck to retain the agarose. 1) Draw (pipet) the desired amount of settled agarose-lectin (gel) from the stock bottle into the prepared column and let the buffer drain by gravity.(Sometimes an air bubble in the column tip prevents flow; tapping the column should get the flow started). 2) Wash the gel with 10 column volumes of buffer, such as HBS (10 mM HEPES, 0.15 M NaCl, pH 7.5) and discard the flow through. 3) Place a collection vessel (e.g. glass test tube) under the column tip and apply the glycoprotein-containing solution.Allow the solution to drain through using gravity. We recommend against pushing or pulling the material through the column. Retain the flow through material until the desired binding has been confirmed. 4) After sample application, wash column with 2-3 column volumes of buffer (or until the absorbance at 280nm is reduced to a satisfactory level) to remove unbound materials before elution. 5) Place a fresh collection vessel under the column tip.Apply the eluting solution again letting gravity do the work of moving the solution over the column. Note that in some cases, several column volumes of eluting solution may be required to achieved adequate release of bound material. 6) Following elution, the column can be prepared for reuse by washing with 10 column volumes of buffer. 7) If the column is to be stored, equilibrate the column with buffer containing 0.08% sodium azide. Cover the column with a plastic wrap, or similar, to prevent desiccation and keep at 4 degrees Celsius. The column will be stable for many months when stored under these conditions.

The pH should be near neutral, the maximum pressure for packing the resin is 10 psi, and the maximum flow rate 3.5 ml/min.

Citations

Technical Information

Con A requires calcium or manganese ions at each of its four saccharide binding sites. Although these divalent metal ions are bound tightly to the polypeptide structure, buffers which can bind calcium (such as phosphate) generally should be avoided in diluting Con A, since a gradual loss in activity may occur.

Agarose bound* Con A is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2×107 daltons are used as the solid-phase matrix to which the lectins are covalently coupled. 

This coupling method provides several advantages over the traditional cyanogen bromide procedure:

  • Maximum carbohydrate binding activity of the coupled lectins is retained
  • Linkage is stable over a range of pH values

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

Inhibiting/Eluting Sugar: mixture of 200 mM α-methylmannoside/200 mM α-methylglucoside or Glycoprotein Eluting Solution (ES-1100)

*6 mg lectin/ml gel

The post Concanavalin A (Con A), Agarose bound appeared first on VectorLabs.

]]> Aleuria Aurantia Lectin (AAL), Agarose bound https://staging.vectorlabs.com/products/agarose-bound-aleuria-aurantia-lectin-aal/ Wed, 19 Apr 2023 16:19:19 +0000 https://staging.vectorlabs.com/?post_type=product&p=10801 Description

Features:

  • Matrix is heat stable, cross-linked 4% agarose beads with a molecular exlusion of about 2×107 daltons
  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Hydrophilic spacer arm is inserted between the lectin and the matrix
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer
  • 2 mg lectin/ml gel
  • Inhibiting/Eluting Sugar: 100 mM L-fucose or Glycoprotein Eluting Solution (ES-3100)

Specifications

Unit Size 2 ml
Applications Glycobiology, Affinity Chromatography
Recommended Storage 2-8 °C DO NOT FREEZE
Solution 10 mM HEPES, pH 7.5, 0.15 M NaCl, 10 mM fucose, 0.08% sodium azide
Recommended Usage Wash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting Solution, Cat. No. ES-3100. Alternatively, 100 mM L-fucose in buffered saline can be used. After use, wash the gel with several column volumes of buffered saline then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix Conjugate Lectins
Sugar Specificity Fucose, Arabinose
Conjugate Agarose

Technical Information

This lectin is a dimer of two identical subunits of about 36 kDa each. Unlike Ulex europaeus and Lotus tetragonolobus lectins which prefer (α -1,2) linked fucose residues, Aleuria aurantia lectin binds preferentially to fucose linked (α -1,6) to N-acetylglucosamine or to fucose linked (α -1,3) to N-acetyllactosamine related structures. AAL also reversibly binds fucose attached to nucleic acids

Agarose bound* Aleuria Aurantia lectin is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2×107 daltons are used as the solid-phase matrix to which the lectins are covalently coupled. The attachment of the lectins to the beads is carefully controlled to preserve lectin activity and minimize conformational changes of the bound lectins that might result in nonspecific ionic or hydrophobic interactions. The technique we have developed to couple lectins to agarose beads inserts a hydrophilic spacer arm between the lectin and the matrix.

This coupling method provides several advantages over the traditional cyanogen bromide procedure:

  • Maximum carbohydrate binding activity of the coupled lectins is retained
  • Linkage is stable over a range of pH values
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges are present after conjugation. This minimizes non-specific binding to the matrix.

 

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

Inhibiting/Eluting Sugar: 100 mM L-fucose

*2 mg lectin/ml gel

The post Aleuria Aurantia Lectin (AAL), Agarose bound appeared first on VectorLabs.

]]>

Description

Features:

  • Matrix is heat stable, cross-linked 4% agarose beads with a molecular exlusion of about 2×107 daltons
  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Hydrophilic spacer arm is inserted between the lectin and the matrix
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer
  • 2 mg lectin/ml gel
  • Inhibiting/Eluting Sugar: 100 mM L-fucose or Glycoprotein Eluting Solution (ES-3100)

Specifications

Unit Size2 ml
ApplicationsGlycobiology, Affinity Chromatography
Recommended Storage2-8 °C DO NOT FREEZE
Solution10 mM HEPES, pH 7.5, 0.15 M NaCl, 10 mM fucose, 0.08% sodium azide
Recommended UsageWash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting Solution, Cat. No. ES-3100. Alternatively, 100 mM L-fucose in buffered saline can be used. After use, wash the gel with several column volumes of buffered saline then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix ConjugateLectins
Sugar SpecificityFucose, Arabinose
ConjugateAgarose

Documents

Product FAQs

Our agarose lectin products are supplied as hydrated matrix solutions in amber glass bottles. The agarose (bead) material will settle and you will see two phases in the tube supplied. The upper phase is buffer. A column can be prepared in a commercial plastic device such as Bio-Rad Cat # 732-6008 or an inverted Pasteur pipet with glass wool lightly packed in the neck to retain the agarose. 1) Draw (pipet) the desired amount of settled agarose-lectin (gel) from the stock bottle into the prepared column and let the buffer drain by gravity.(Sometimes an air bubble in the column tip prevents flow; tapping the column should get the flow started). 2) Wash the gel with 10 column volumes of buffer, such as HBS (10 mM HEPES, 0.15 M NaCl, pH 7.5) and discard the flow through. 3) Place a collection vessel (e.g. glass test tube) under the column tip and apply the glycoprotein-containing solution.Allow the solution to drain through using gravity. We recommend against pushing or pulling the material through the column. Retain the flow through material until the desired binding has been confirmed. 4) After sample application, wash column with 2-3 column volumes of buffer (or until the absorbance at 280nm is reduced to a satisfactory level) to remove unbound materials before elution. 5) Place a fresh collection vessel under the column tip.Apply the eluting solution again letting gravity do the work of moving the solution over the column. Note that in some cases, several column volumes of eluting solution may be required to achieved adequate release of bound material. 6) Following elution, the column can be prepared for reuse by washing with 10 column volumes of buffer. 7) If the column is to be stored, equilibrate the column with buffer containing 0.08% sodium azide. Cover the column with a plastic wrap, or similar, to prevent desiccation and keep at 4 degrees Celsius. The column will be stable for many months when stored under these conditions.

The pH should be near neutral, the maximum pressure for packing the resin is 10 psi, and the maximum flow rate 3.5 ml/min.

Citations

Technical Information

This lectin is a dimer of two identical subunits of about 36 kDa each. Unlike Ulex europaeus and Lotus tetragonolobus lectins which prefer (α -1,2) linked fucose residues, Aleuria aurantia lectin binds preferentially to fucose linked (α -1,6) to N-acetylglucosamine or to fucose linked (α -1,3) to N-acetyllactosamine related structures. AAL also reversibly binds fucose attached to nucleic acids

Agarose bound* Aleuria Aurantia lectin is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2×107 daltons are used as the solid-phase matrix to which the lectins are covalently coupled. The attachment of the lectins to the beads is carefully controlled to preserve lectin activity and minimize conformational changes of the bound lectins that might result in nonspecific ionic or hydrophobic interactions. The technique we have developed to couple lectins to agarose beads inserts a hydrophilic spacer arm between the lectin and the matrix.

This coupling method provides several advantages over the traditional cyanogen bromide procedure:

  • Maximum carbohydrate binding activity of the coupled lectins is retained
  • Linkage is stable over a range of pH values
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges are present after conjugation. This minimizes non-specific binding to the matrix.

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

Inhibiting/Eluting Sugar: 100 mM L-fucose

*2 mg lectin/ml gel

The post Aleuria Aurantia Lectin (AAL), Agarose bound appeared first on VectorLabs.

]]> Wisteria Floribunda Lectin (WFA, WFL), Agarose bound https://staging.vectorlabs.com/products/agarose-bound-wisteria-floribunda-lectin/ Wed, 19 Apr 2023 16:13:44 +0000 https://staging.vectorlabs.com/?post_type=product&p=10794 Description

Features:

  • Matrix is heat stable, cross-linked 4% agarose beads with a molecular exlusion of about 2×107 daltons
  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Hydrophilic spacer arm is inserted between the lectin and the matrix
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer
  • 3 mg lectin/ml gel
  • Inhibiting/Eluting Sugar: 200 mM N-acetylgalactosamine or Glycoprotein Eluting Solution (ES-2100)

Specifications

Unit Size 2 ml
Applications Glycobiology, Affinity Chromatography
Recommended Storage 2-8 °C DO NOT FREEZE
Solution 10 mM HEPES, pH 7.5, 0.15 M NaCl, 0.1 mM CaCl2, 20 mM galactose, 0.08% sodium azide
Recommended Usage Wash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting solution, Cat. No. ES-2100. Alternatively, 200 mM N-acetylgalactoseamine or several column volumes of 200 mM acetic acid can be used. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix Conjugate Lectins
Sugar Specificity N-Acetylgalactosamine
Conjugate Agarose

Technical Information

The binding specificity of Wisteria floribunda lectin (WFL) is not completely clear but this lectin appears to preferentially bind carbohydrate structures terminating in N-acetylgalactosamine linked α or β to the 3 or 6 position of galactose. This lectin has been used to fractionate lymphocyte populations, and although not mitogenic, elicits the production of lymphokines from murine splenocytes.

Agarose bound* WFL is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2×107 daltons are used as the solid-phase matrix to which the lectins are covalently coupled. The attachment of the lectins to the beads is carefully controlled to preserve lectin activity and minimize conformational changes of the bound lectins that might result in nonspecific ionic or hydrophobic interactions. The technique we have developed to couple lectins to agarose beads inserts a hydrophilic spacer arm between the lectin and the matrix.

This coupling method provides several advantages over the traditional cyanogen bromide procedure:

  • Maximum carbohydrate binding activity of the coupled lectins is retained
  • Linkage is stable over a range of pH values
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges are present after conjugation. This minimizes non-specific binding to the matrix.

 

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

Inhibiting/Eluting Sugar: 200 mM N-acetylgalactosamine

*3 mg lectin/ml gel

The post Wisteria Floribunda Lectin (WFA, WFL), Agarose bound appeared first on VectorLabs.

]]>

Description

Features:

  • Matrix is heat stable, cross-linked 4% agarose beads with a molecular exlusion of about 2×107 daltons
  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Hydrophilic spacer arm is inserted between the lectin and the matrix
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer
  • 3 mg lectin/ml gel
  • Inhibiting/Eluting Sugar: 200 mM N-acetylgalactosamine or Glycoprotein Eluting Solution (ES-2100)

Specifications

Unit Size2 ml
ApplicationsGlycobiology, Affinity Chromatography
Recommended Storage2-8 °C DO NOT FREEZE
Solution10 mM HEPES, pH 7.5, 0.15 M NaCl, 0.1 mM CaCl2, 20 mM galactose, 0.08% sodium azide
Recommended UsageWash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting solution, Cat. No. ES-2100. Alternatively, 200 mM N-acetylgalactoseamine or several column volumes of 200 mM acetic acid can be used. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix ConjugateLectins
Sugar SpecificityN-Acetylgalactosamine
ConjugateAgarose

Documents

Product FAQs

Our agarose lectin products are supplied as hydrated matrix solutions in amber glass bottles. The agarose (bead) material will settle and you will see two phases in the tube supplied. The upper phase is buffer. A column can be prepared in a commercial plastic device such as Bio-Rad Cat # 732-6008 or an inverted Pasteur pipet with glass wool lightly packed in the neck to retain the agarose. 1) Draw (pipet) the desired amount of settled agarose-lectin (gel) from the stock bottle into the prepared column and let the buffer drain by gravity.(Sometimes an air bubble in the column tip prevents flow; tapping the column should get the flow started). 2) Wash the gel with 10 column volumes of buffer, such as HBS (10 mM HEPES, 0.15 M NaCl, pH 7.5) and discard the flow through. 3) Place a collection vessel (e.g. glass test tube) under the column tip and apply the glycoprotein-containing solution.Allow the solution to drain through using gravity. We recommend against pushing or pulling the material through the column. Retain the flow through material until the desired binding has been confirmed. 4) After sample application, wash column with 2-3 column volumes of buffer (or until the absorbance at 280nm is reduced to a satisfactory level) to remove unbound materials before elution. 5) Place a fresh collection vessel under the column tip.Apply the eluting solution again letting gravity do the work of moving the solution over the column. Note that in some cases, several column volumes of eluting solution may be required to achieved adequate release of bound material. 6) Following elution, the column can be prepared for reuse by washing with 10 column volumes of buffer. 7) If the column is to be stored, equilibrate the column with buffer containing 0.08% sodium azide. Cover the column with a plastic wrap, or similar, to prevent desiccation and keep at 4 degrees Celsius. The column will be stable for many months when stored under these conditions.

The pH should be near neutral, the maximum pressure for packing the resin is 10 psi, and the maximum flow rate 3.5 ml/min.

Citations

Technical Information

The binding specificity of Wisteria floribunda lectin (WFL) is not completely clear but this lectin appears to preferentially bind carbohydrate structures terminating in N-acetylgalactosamine linked α or β to the 3 or 6 position of galactose. This lectin has been used to fractionate lymphocyte populations, and although not mitogenic, elicits the production of lymphokines from murine splenocytes.

Agarose bound* WFL is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2×107 daltons are used as the solid-phase matrix to which the lectins are covalently coupled. The attachment of the lectins to the beads is carefully controlled to preserve lectin activity and minimize conformational changes of the bound lectins that might result in nonspecific ionic or hydrophobic interactions. The technique we have developed to couple lectins to agarose beads inserts a hydrophilic spacer arm between the lectin and the matrix.

This coupling method provides several advantages over the traditional cyanogen bromide procedure:

  • Maximum carbohydrate binding activity of the coupled lectins is retained
  • Linkage is stable over a range of pH values
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges are present after conjugation. This minimizes non-specific binding to the matrix.

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

Inhibiting/Eluting Sugar: 200 mM N-acetylgalactosamine

*3 mg lectin/ml gel

The post Wisteria Floribunda Lectin (WFA, WFL), Agarose bound appeared first on VectorLabs.

]]> Sambucus Nigra Lectin (SNA, EBL), Agarose bound https://staging.vectorlabs.com/products/agarose-bound-sambucus-nigra-lectin-sna-ebl/ Tue, 18 Apr 2023 20:58:59 +0000 https://staging.vectorlabs.com/?post_type=product&p=10782 Description

Agarose bound Sambucus nigra lectin is prepared using our affinity-purified lectins. Sambucus nigra lectin, isolated from elderberry bark, binds preferentially to sialic acid attached to terminal galactose in α-2,6 and to a lesser degree, α-2,3 linkage. Binding is also inhibited to some extent by lactose or galactose. This lectin appears to bind sialic acid linked to N-acetylgalactosamine or galactose.

Features:

  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Hydrophilic spacer arm is inserted between the lectin and the matrix
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer
  • 3 mg lectin/ml gel
  • 500 mM lactose in buffered saline followed by 500 mM lactose in acetic acid or Glycoprotein Eluting Solution (ES-7100)

Specifications

Unit Size 2 ml
Applications Glycobiology, Affinity Chromatography
Recommended Storage 2-8 °C DO NOT FREEZE
Solution 10 mM HEPES, pH 7.5, 0.15 M NaCl, 0.1 mM CaCl2, 0.08% sodium azide, 20 mM lactose
Recommended Usage Wash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting Solution, Cat. No. ES-7100. Alternatively, 0.5 M lactose in buffered saline followed by 0.5 M lactose in 0.2 M acetic acid can be used. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline, containing 0.08% sodium azide for storage.
Matrix Conjugate Lectins
Sugar Specificity Sialic Acid
Conjugate Agarose

Technical Information

Our coupling method provides several advantages over the traditional cyanogen bromide procedure:

  • Maximum carbohydrate binding activity of the coupled lectins is retained
  • Linkage is stable over a range of pH values
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges are present after conjugation. This minimizes non-specific binding to the matrix.

 

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

Elution: 500 mM lactose in buffered saline followed by 500 mM lactose in acetic acid

The post Sambucus Nigra Lectin (SNA, EBL), Agarose bound appeared first on VectorLabs.

]]>

Description

Agarose bound Sambucus nigra lectin is prepared using our affinity-purified lectins. Sambucus nigra lectin, isolated from elderberry bark, binds preferentially to sialic acid attached to terminal galactose in α-2,6 and to a lesser degree, α-2,3 linkage. Binding is also inhibited to some extent by lactose or galactose. This lectin appears to bind sialic acid linked to N-acetylgalactosamine or galactose. 

Features:

  • Bead diameter ranges in size from 45-165 microns
  • Matrix is stable in solutions at pH 3-11 as well as many organic solvents
  • Immobilized lectins are prepared using affinity purified lectins
  • Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
  • Hydrophilic spacer arm is inserted between the lectin and the matrix
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges present after conjugation.  This minimizes non-specific binding to the matrix
  • Product supplied as a 1:1 suspension in buffer
  • 3 mg lectin/ml gel
  • 500 mM lactose in buffered saline followed by 500 mM lactose in acetic acid or Glycoprotein Eluting Solution (ES-7100)

Specifications

Unit Size2 ml
ApplicationsGlycobiology, Affinity Chromatography
Recommended Storage2-8 °C DO NOT FREEZE
Solution10 mM HEPES, pH 7.5, 0.15 M NaCl, 0.1 mM CaCl2, 0.08% sodium azide, 20 mM lactose
Recommended UsageWash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting Solution, Cat. No. ES-7100. Alternatively, 0.5 M lactose in buffered saline followed by 0.5 M lactose in 0.2 M acetic acid can be used. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline, containing 0.08% sodium azide for storage.
Matrix ConjugateLectins
Sugar SpecificitySialic Acid
ConjugateAgarose

Documents

Product FAQs

Our agarose lectin products are supplied as hydrated matrix solutions in amber glass bottles. The agarose (bead) material will settle and you will see two phases in the tube supplied. The upper phase is buffer. A column can be prepared in a commercial plastic device such as Bio-Rad Cat # 732-6008 or an inverted Pasteur pipet with glass wool lightly packed in the neck to retain the agarose. 1) Draw (pipet) the desired amount of settled agarose-lectin (gel) from the stock bottle into the prepared column and let the buffer drain by gravity.(Sometimes an air bubble in the column tip prevents flow; tapping the column should get the flow started). 2) Wash the gel with 10 column volumes of buffer, such as HBS (10 mM HEPES, 0.15 M NaCl, pH 7.5) and discard the flow through. 3) Place a collection vessel (e.g. glass test tube) under the column tip and apply the glycoprotein-containing solution.Allow the solution to drain through using gravity. We recommend against pushing or pulling the material through the column. Retain the flow through material until the desired binding has been confirmed. 4) After sample application, wash column with 2-3 column volumes of buffer (or until the absorbance at 280nm is reduced to a satisfactory level) to remove unbound materials before elution. 5) Place a fresh collection vessel under the column tip.Apply the eluting solution again letting gravity do the work of moving the solution over the column. Note that in some cases, several column volumes of eluting solution may be required to achieved adequate release of bound material. 6) Following elution, the column can be prepared for reuse by washing with 10 column volumes of buffer. 7) If the column is to be stored, equilibrate the column with buffer containing 0.08% sodium azide. Cover the column with a plastic wrap, or similar, to prevent desiccation and keep at 4 degrees Celsius. The column will be stable for many months when stored under these conditions.

The pH should be near neutral, the maximum pressure for packing the resin is 10 psi, and the maximum flow rate 3.5 ml/min.

Citations

Technical Information

Our coupling method provides several advantages over the traditional cyanogen bromide procedure:

  • Maximum carbohydrate binding activity of the coupled lectins is retained
  • Linkage is stable over a range of pH values
  • Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
  • No residual charges are present after conjugation. This minimizes non-specific binding to the matrix.

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

Elution: 500 mM lactose in buffered saline followed by 500 mM lactose in acetic acid

The post Sambucus Nigra Lectin (SNA, EBL), Agarose bound appeared first on VectorLabs.

]]>