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Pisum sativum agglutinin is nearly identical in structure and carbohydrate specificity to Lens culinaris agglutinin. PSA has four subunits, two of approximately 17,000 daltons and two of about 6,000 daltons. Isoelectric focusing has revealed two isolectins with isoelectric points of pH 5.9 and pH 7.0. The lectin has specificity toward a-linked mannose-containing oligosaccharides, with an N-acetylchitobiose-linked a-fucose residue included in the receptor sequence. Calcium and manganese ions are required for activity. PSA has been used to fractionate cells, to isolate glycoproteins and glycopeptides, to distinguish between normal and virally transformed cells, as a T-cell mitogen, and as an inhibitor of allograft rejection.
Rhodamine labeled Pisum Sativum Agglutinin is produced by using the highest quality tetramethylrhodamine isothiocyanate, our affinity-purified lectin, and special conjugation procedures. Rhodamine labeled Pisum Sativum Agglutinin has an appropriate number of fluorochromes bound which provide the maximum fluorescence and optimum staining characteristics for this particular lectin. This lectin is supplied essentially free of unconjugated fluorochromes and inactive lectin. Rhodamine labeled Pisum Sativum Agglutinin has an absorption maximum at about 550 nm and a maximum emission at about 575 nm. |