Phaseolus vulgaris Lectin (PHA-E) - Pure
Phaseolus vulgaris lectin (PHA-E) is isolated from red kidney bean seeds and is responsible for the erythroagglutinating properties of the PHA fraction. It is a tetrameric glycoprotein with a molecular weight of 126,000 and an isoelectric point around pH 6.0. It has a carbohydrate specificity towards oligosaccharides and elutes with 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. The crystal structure of a ligand-free PHA-E has a typical legume lectin fold characterized by two anti-parallel ?-sheets and two short ?-helices, and contains one GlcNAc residue of the N-linked glycan.
Asparagine linked erythrocytes glycopeptide is an inhibitor of PHA-E induced agglutination and mitogenicity, and becomes inactive if treated with ?-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 form and is stable for more than three years when stored below -20ºC. Metal ions calcium and manganese are required for binding activity.