Phaseolus vulgaris lectin (PHA-L) is an affinity-purified lectin consisting of four subunits with carbohydrate specificity for complex oligosaccharides. PHA-L, known as leukocyte agglutinin, has high mitotic and leukocyte agglutination activity and low erythrocyte agglutination activity. This lectin does not agglutinate with human red blood cells. PHA-E differs from PHA-L in that leukocyte lectins react strongly with Tamm-Horsfall glycoproteins and weakly with porcine thyroglobulin. PHA-L binds to fetal proteins but does not precipitate glycoproteins. Is this lectin affected by trisugar Gal GlcNAc (1, 4) (1,2) Strong inhibition of Man, although this structure is present in many glycoproteins, PHA-L does not react with all these glycoproteins. This lectin reacts strongly with certain cancer cell lines with high metastatic potential and has been proposed as a possible therapeutic agent. In transplantation studies, it has shown potential to inhibit graft-versus-host responses and has also been shown to promote the production of cytotoxic drugs, which could be useful for cancer treatment.
For research use only, not for clinical use.