Griffonia simplicifolia Lectin (GSL I) - Pure

Product Description
Pure lectin GSL I is isolated from bandeiraea, Griffonia simplicifolia and purified by affinity chromatography. GSL I has a molecular weight of 114,000 and isoelectric points from pH 5 to 6.5. GSL I is composed of two types of subunits A and B that combine to form tetrameric structures, resulting in five isolectins. This lectin has affinity for terminal α-D-galactosyl residues and terminal N-acetyl-α-D-galactosaminyl residues, and elutes a concentration of 0.2M of galactose. 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. The lectin shows specificity for blood group B greater than blood group A₁.

GSL I has been reported to bind several glycoproteins including laminin. Studies show that some α-D-galactosyl residues are expressed in endothelial cells of mouse tissues and provide evidence that endothelial cells can present a highly specific surface glycosylation pattern.

This product comes in lyophilized powder form and is stored at -20 C. Reconstitute with sterile buffer. Calcium and manganese are required for binding.

Applications:
Immunohistochemistry/immunocytochemistry
Immunofluorescence
Blotting applications
Glycobiology

References

• Purified by affinity chromatography using the method of Hayes, E., and Goldstein, J. J. Biol. Chem. (1974) 249:1904.
• Laitinen, L. Griffonia simplicifolia lectins bind specifically to endothelial cells and some epithelial cells in mouse tissues. Histochem J. (1987) 19(4):225-34.