Agarose-GLAGLLAR-Alkyne is an agarose resin that is pre-activated with terminal alkyne groups linked to the agarose resin through a short synthetic peptide containing a tryptic cleavage site. The azide-modified proteins, or their post-translationally modified forms, are captured from complex protein extracts on the Agarose-GLAGLLAR-Alkyne resin. Once covalently attached to the resin via copper catalyzed click chemistry, beads can be washed with highest stringency virtually eliminating any non-specifically bound proteins to yield a highly enriched population of nascent molecules. Upon tryptic digestion, this yields a highly pure peptide pool that is ideal for mass spectrometry (e.g., LC MS/MS) based analysis. Importantly, azide-modified targeted peptides can be easily identified by MS analysis, providing a confirmation by a mass shift of 113.05 Da

Specifications

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Agarose-GLAGLLAR-Azide is an agarose resin that is pre-activated with azide groups linked to the agarose resin through a short synthetic peptide containing a tryptic cleavage site. The alkyne-modified proteins, or their post-translationally modified forms, are captured from complex protein extracts on the Agarose-GLAGLLAR-Azide resin. Once covalently attached to the resin via copper catalyzed click chemistry, beads can be washed with highest stringency virtually eliminating any non-specifically bound proteins to yield a highly enriched population of nascent molecules. Upon tryptic digestion, this yields a highly pure peptide pool that is ideal for mass spectrometry (e.g., LC MS/MS) based analysis. Importantly, alkyne-modified targeted peptides can be easily identified by MS analysis, providing a confirmation by a mass shift of 172.10 Da

Specifications

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Methyltetrazine-activated, highly uniform polymer-based magnetic spheres of 1 µm diameter. A unique surface means low nonspecific binding in protein-based systems, and superior handling without the use of surfactant. These high-binding beads are suitable for use across a range of research and diagnostic applications, whether you’re working at laboratory scale or have the more stringent requirements of high throughput applications.

Specifications

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Picolyl Azide Agarose is a 6% crosslinked agarose resin that is activated with picolyl azide functional groups for covalent capturing alkyne-tagged biomolecules. Picolyl Azide incorporates a copper-chelating motif to raise the effective concentration of Cu(I) at the reaction site to boosted the efficiency of the CuAAC reaction resulting in a faster and more biocompatible CuAAC labeling. Up to 40-fold increase of signal intensity, compared to conventional azides was reported (see Selected References).This product is adequate to work in batch or column purification (low pressure).

Specifications

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Additional points:

Binding capacity: ≥ 12 nmol/mg of free biotin per mg of beads and ≥ 110 µg/mg of biotinylated IgG per mg of beads.

Excellent for fast and direct isolation of any biotinylated molecules, such as nucleic acids (both DNA and RNA), oligonucleotides, proteins, peptides, and antibodies.

Easily adapted for manual and automated high-throughput applications.

High batch-to-batch reproducibility.

30 µg of BSA-biotin in HEK 293T RIPA lysate was mixed with 1 mg of High Capacity Streptavidin Magnetic Beads. Eluted with 1x Laemmli Sample Buffer, 10 minutes at 95 C. Mass shift – conjugate of BSA-biotin and one subunit of Streptavidin.

Specifications

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PC Azide Agarose is a 6% crosslinked agarose resin that is activated with azide groups through a photocleavable linker. Once biomolecules are covalently captures to the resin, beads can be washed with highest stringency virtually eliminating any non-specifically bound proteins. Irradiation with a hand-held UV-Vis lamp allows for reagent-less release of captured molecules. This product is adequate to work in batch or column purification (low pressure).

Specifications

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PC Alkyne Agarose is a 6% crosslinked agarose resin that is activated with alkyne groups through a photocleavable linker. Once biomolecules are covalently captures to the resin, beads can be washed with highest stringency virtually eliminating any non-specifically bound proteins. Irradiation with a hand-held UV-Vis lamp allows for reagent-less release of captured molecules. This product is adequate to work in batch or column purification (low pressure).

Specifications

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Extraordinary strength of the streptavidin-biotin interaction allows for efficient capturing of even highly dilute targets; however, it makes recovery of proteins from affinity resins challenging. Conventional methods to elute biotinylated proteins from immobilized avidin include the following: (i) denaturation of streptavidin by boiling the resin in a denaturing buffer that may include high concentrations of chaotropic salts, (ii) trypsin digestion of proteins while they are bound to the resin, or (iii) elution of proteins with excess free biotin. These protocols can co-elute contaminant proteins by releasing nonspecifically bound proteins and/or naturally biotinylated proteins concurrently with labeled proteins. In addition, some of these methods can cause elution of high levels of resin-based peptides along with the proteins of interest, resulting in further sample contamination.

Dde Biotin Azide probe eliminates a major limitation of the streptavidin-biotin affinity purification. This reagent contains a biotin moiety linked to an azide (N3) through a spacer arm containing a containing a hydrazine-cleavable Dde moiety. Captured biomolecules can be efficiently released under mild conditions (2% aqueous hydrazine solution), and the small molecular fragment (100.07 Da) left on the labeled protein following the cleavage. These features make the cleavable probe especially attractive for use in biomolecular labeling and proteomic studies.

Specifications

[caption id="attachment_26280" align="alignnone" width="380"] Schematic Workflow[/caption]

The post Click-&-Go® Dde Protein Enrichment Kit appeared first on VectorLabs.

Extraordinary strength of the streptavidin-biotin interaction allows for efficient capturing of even highly dilute targets; however, it makes recovery of proteins from affinity resins challenging. Conventional methods to elute biotinylated proteins from immobilized avidin include the following: (i) denaturation of streptavidin by boiling the resin in a denaturing buffer that may include high concentrations of chaotropic salts, (ii) trypsin digestion of proteins while they are bound to the resin, or (iii) elution of proteins with excess free biotin. These protocols can co-elute contaminant proteins by releasing nonspecifically bound proteins and/or naturally biotinylated proteins concurrently with labeled proteins. In addition, some of these methods can cause elution of high levels of resin-based peptides along with the proteins of interest, resulting in further sample contamination.

Dde Biotin Alkyne probe eliminates a major limitation of the streptavidin-biotin affinity purification. This reagent contains a biotin moiety linked to an azide (N3) through a spacer arm containing a containing a hydrazine-cleavable Dde moiety. Captured biomolecules can be efficiently released under mild conditions (2% aqueous hydrazine solution), and the small molecular fragment (55.07 Da) left on the labeled protein following the cleavage. These features make the cleavable probe especially attractive for use in biomolecular labeling and proteomic studies.

Specifications

[caption id="attachment_26280" align="alignnone" width="380"] Schematic Workflow[/caption]

The post Click-&-Go® Dde Protein Enrichment Kit appeared first on VectorLabs.

Extraordinary strength of the streptavidin-biotin interaction allows for efficient capturing of even highly dilute targets; however, it makes recovery of proteins from affinity resins challenging. Conventional methods to elute biotinylated proteins from immobilized avidin include the following: (i) denaturation of streptavidin by boiling the resin in a denaturing buffer that may include high concentrations of chaotropic salts, (ii) trypsin digestion of proteins while they are bound to the resin, or (iii) elution of proteins with excess free biotin. These protocols can co-elute contaminant proteins by releasing nonspecifically bound proteins and/or naturally biotinylated proteins concurrently with labeled proteins. In addition, some of these methods can cause elution of high levels of resin-based peptides along with the proteins of interest, resulting in further sample contamination.

DADPS (dialkoxydiphenylsilane) Biotin Azide probes eliminate a major limitation of the streptavidin-biotin affinity purification. This reagent contains a biotin moiety linked to an azide moiety through a spacer arm containing a cleavable DADPS linker. Captured biomolecules can be efficiently released under mild conditions (10% formic acid, 0.5 h) and the small (143 Da) molecular fragment left on the labeled protein following cleavage. These features make the DADPS probe especially attractive for use in biomolecular labeling and proteomic studies.

Specifications

[caption id="attachment_26280" align="alignnone" width="380"] Schematic Workflow[/caption]

The post Click-&-Go® DADPS Protein Enrichment Kit appeared first on VectorLabs.