Phaseolus vulgaris Lectin (PHA-L) - Pure

Product Description
This lectin (PHA-L) is isolated from red kidney beans, Phaseolus vulgaris. It has a molecular weight of 126,000 Da and is made up of four subunits. This lectin has an isoelectric point of pH 4.2 - 4.8 and a carbohydrate specificity for complex oligosaccharides, and elutes a concentration of 0.2M of bovine thyroglobulin or acetic acid.

PHA-L is known as leucoagglutinin and has high mitogenic and leucoagglutinating activity but low erythroagglutinating activity. This lectin exhibits no agglutination with human erythrocytes.

Differences from PHA-E is that PHA-L reacts strongly with Tamm-Horsfall glycoprotein and reacts weakly with porcine thyroglobulin. PHA-L binds to fetuin but does not precipitate the glycoprotein. This lectin is strongly inhibited by trisaccharide Gal Beta(1,4)GlcNAcBeta(1,2)Man, and although this structure is present in many glycoproteins, PHA-L does not react with all of those.

This lectin reacts strongly with certain carcinoma cell lines of high metastatic potential and has been proposed as a potential therapeutic agent. It has shown potential to inhibit graft vs. host reaction in transplantation studies and has also shown to promote the production of cytotoxic agents which could be useful in cancer therapy. PHA-L has been used in preliminary studies indicating that it is a good biological response modifier.

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

Applications:
Leucocyte agglutination studies
Mammalian glycoprotein studies
Model system of how proteins recognize carbohydrates
Anterograde transport studies

References

• Liener E., et al. The lectins - properties, functions and applications in biology and medicine. (1986).
• Movafagh, A., et al. The significance application of indigenous phytohemagglutinin (PHA) mitogen on metaphase and cell culture procedure. Iran J Pharm Res. (2011) 10(4):895-903.