Phaseolus vulgaris lectin L

Phaseolus vulgaris lectin L (PHA-L) is isolated from red kidney beans and purified by affinity chromatography. It is a tetrameric protein with a molecular weight of 126 kDa, each subunit of about 31 kDa. The lectin recognizes and binds specifically to terminal galactose, N-acetylglucosamine and mannose residues of complex glycans on mammalian glycoproteins. PHA-L is also known as leucoagglutinin and has high mitogenic and leucoagglutinating activity, but low erythroagglutinating activity. The lectin recognizes terminal galactose residues of complex glycans on mammalian glycoproteins such as thyroglobulin. PHA-L does not agglutinate human erythrocytes at concentrations of 250µg/mL or less, and is non-specific for blood groups. PHA-L lectin is supplied as a white lyophilized powder from a buffer containing from 10mM NH4HCO3. The purity of the lectin is determined by SDS-PAGE generating one single band at 31 kDa. It is available in vials containing 2mg or 10mg lyophilized powder and the product is to be used for laboratory work only.