Phaseolus vulgaris lectin L (PHA-L)
*** For pack size 1g or more, please contact us to inquire about pricing
- Ultrapure quality
- Sugar specificity: complex oligosaccharides
- High mitogenic and leucoagglutinating activity
- Very low erythroagglutinating activity
- Lyophilized powder
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 (1).
PHA-L is also known as leucoagglutinin and has high mitogenic and leucoagglutinating activity, but low erythroagglutinating activity (1). The lectin recognizes terminal galactose residues of complex glycans on mammalian glycoproteins such as thyroglobulin (3). PHA-L does not agglutinate human erythrocytes at concentrations of 250 µg/ml or less, and is non-specific for blood groups.
Medicago’s PHA-L lectin is supplied as a white lyophilized powder from a buffer containing from 10 mM NH4HCO3. The purity of the lectin is determined by SDS-PAGE generating one single band at 31 kDa. It is available in vials containing 10 mg or 2 mg lyophilized powder and the product is to be used for laboratory work only.
- Leucocyte agglutination studies
- Mammalian glycoprotein studies
- Model system of how proteins recognize carbohydrates
Directions for use
The lectin may be reconstituted with 2 ml of deionized water before use. Spin the vial gently until full dissolution. Aggregation is thought to occur in the presence of high concentrations of 2-mercaptoethanol. The solution may be reconstituted in this buffer to desired working concentration.
Shipping and storage
The product is shipped at -20°C however for over-the-day transport it may be shipped at ambient temperature. The lyophilized powder is stable for more than three years from production date when stored below -20°C. After reconstitution with deionized water, the solution may be stored frozen in working aliquots for up to 12 months.
(1) Liener I. E., Sharon N., Goldstein I. J., (1986) The Lectins – Properties, Functions and Applications in Biology and Medicine.
(2) Weak protein-protein interactions in lectins: the crystal structure of a vegetative lectin from the legume Dolichos biflorus. Buts, L., Dao-Thi, M.H., Loris, R., Wyns, L., Etzler, M., Hamelryck, T. (2001) J.Mol.Biol. 309: 193–201.
(3) Chrispeels M. J., Raikhel N. V. (1991). Lectins, Lectin Genes, and Their Role in Plant Defense. The Plant Cell Vol.3, 1–9.