Affinity Purified Phaseolus vulgaris lectin (PHA E+L, also known as PHA P, P standing for phytohemagglutinin) is affinity purified lectin consists of two isolectins PHA-E and PHA-L, erythroagglutinin and leucoagglutinin, of which both possess strong mitogenic activity. PHA P has a molecular weight of 126,000 and an isoelectric point between pH 5.2 and pH 6.2. It has a carbohydrate specificity for complex oligosaccharides and elutes with bovine thyroglobulin or acetic acid. This lectin agglutinates blood group A (-SA).
PHA P can be used for mitogenic stimulation to human lymphocytes. It has the potential to induce closer contacts between adjacent cell membranes and has been successfully used for membrane-induced fusion in human oocytes, bovine oocyt, and caprine oocytes. Phytohemagglutinin was direct evidence for the involvement of bacterial lectins in the initiation of infection, the basis for present attempts in academia and industry to apply carbohydrates for anti-adhesion therapy of such diseases.
Alkaline phosphatase (AP) is conjugated to Phaseolus vulgaris Lectin (PHA-E+L) to show the binding of PHA-E+L in many applications including Western blotting and ELISA. Alkaline phosphatase is a large protein (140 kDa) that catalyzes the hydrolysis of phosphate groups from a substrate resulting in a colored or fluorescent product. The optimal enzymatic activity of this protein is between pH 8 and 10, and its reaction rate remains linear, improving sensitivity over time.