Phaseolus vulgaris agglutinin is the name ascribed to a family of lectins, each of which consists of four subunits. There are two different types of subunits. One appears to be involved primarily in red cell agglutination and has been designated the “E” subunit (for erythroagglutinin). The other type is involved in lymphocyte agglutination and mitogenic activity and has been termed the “L” subunit (for leucoagglutinin). These subunits combine to produce five isolectins.  PHA-L, with four “L” type subunits, does not agglutinate red cell but is a potent mitogen.

Rhodamine labeled PHA-L has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated fluorochromes. The excitation maximum is at 550 nm and the emission maximum is at 575 nm.

GSL I is a family of glycoproteins with molecular weights of approximately 114 kDa. There are two types of subunits, termed “A” and “B”, with slightly different molecular weights. These subunits combine to form tetrameric structures, resulting in five isolectins. The “A”-rich lectin preferentially agglutinates blood group A erythrocytes and thus appears to be specific for α-N-acetylgalactosamine residues, while the “B”-rich lectin preferentially agglutinates blood group B cells and is specific for α-galactose residues. Our GSL I is a mixture of the five isolectins. GSL I has been reported to bind several glycoproteins including laminin.

Rhodamine labeled GSL I has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated fluorochromes. The excitation maximum is at 550 nm and the emission maximum is at 575 nm.

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.  The B chain binds to galactose or N-acetylgalactosamine residues of membrane glycoconjugates.

Rhodamine labeled Ricinus communis agglutinin I has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated fluorochromes. The excitation maximum is at 550 nm and the emission maximum is at 575 nm.

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.

Rhodamine labeled Peanut agglutinin has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated fluorochromes. The excitation maximum is at 550 nm and the emission maximum is at 575 nm.

Ulex europaeus agglutinin I binds to many glycoproteins and glycolipids containing α-linked fucose residues, such as ABO blood group glycoconjugates. This lectin preferentially binds blood group O cells and has been used to determine secretor status. It has been established as an excellent marker for human endothelial cells.

Rhodamine labeled Ulex europaeus agglutinin I has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated fluorochromes. The excitation maximum is at 550 nm and the emission maximum is at 575 nm.

This lectin has a carbohydrate specificity toward α-linked N-acetylgalactosamine.  It has been used to establish secretor status in blood group A individuals by hemagglutination inhibition techniques and for blood typing. This lectin has also been used as a general marker of developing renal collecting ducts.

Rhodamine labeled Dolichos biflorus agglutinin has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated fluorochromes. The excitation maximum is at 550 nm and the emission maximum is at 575 nm.

Con A recognizes α-linked mannose present as part of a “core oligosaccharide” in many serum and membrane glycoproteins.

Rhodamine labeled Con A has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated fluorochromes. The excitation maximum is at 550 nm and the emission maximum is at 575 nm.