Phaseolus vulgaris Lectin (PHA-E) - Pure

Product Description
Pure lectin PHA-E is isolated from red kidney bean seeds, Phaseolus vulgaris, and is responsible for the erythroagglutinating properties of the PHA fraction. The crystal structure of a ligand-free PHA-E has a typical legume lectin fold characterized by two anti-parallel Beta-sheets and two short α-helices, and contains one GlcNAc residue of the N-linked glycan.

PHA-E is a tetrameric glycoprotein with a molecular weight of 126,000 Da. This lectin has an isoelectric point of pH 6 - 8 and a carbohydrate specificity towards oligosaccharides, and elutes a concentration of 0.2M of bovine thyroglobulin or acetic acid. PHA-E will bind to both human erythrocytes and lymphocytes, with a specificity towards blood group A (-SA). There are five times more PHA-E receptors on normal human lymphocytes than there are on erythrocytes.

Asparagine linked erythrocytes glcopeptide is an inhibitor of PHA-E induced agglutination and mitogencity, but will become inactive if treated with Beta-galactosidase, although the lectin is not inhibited.

PHA-E binds di-galactosylated and bisected N-glycan. This lectin is widely used as a biochemical tool for detecting bisecting GlcNAc- and Gal-bearing glycoproteins.

This product comes in a lyophilized powder form and is stable for more than three years from production date when stored below -20 C. Metal ions calcium and manganese are required for binding activity.

Applications:
Erythrocyte agglutination studies
Model system of how proteins recognize carbohydrates

References

• Nagae, M., et al. Phytohemagglutinin from Phaseolus vulgaris (PHA-E) displays a novel glycan recognition mode using a common legume lectin fold. Glycobiology. (2014) 24(4):368-378.