Lens culinaris agglutinin has a molecular weight of approximately 49,000 and is composed of four subunits-two of about 17,000D and two of 8,000D. The isoelectric point of LCA is approximately pH 8.5. LCA recognizes sequences containing a-linked mannose residues. Like other mannose specific lectins, divalent cations such as calcium and manganese are required for sugar binding activity. By recognizing additional sugars as part of the receptor structure, LCA has a narrower specificity than Con A. For example, an a-linked fucose residue attached to the N-acetylchitobiose portion of the core oligosaccharide markedly enhances affinity. By exploiting this narrower specificity, glycoproteins and glycopeptides can be subfractionated with LCA after initial isolation with Con A. LCA has been employed to separate lymphocyte populations, as a potent T-cell mitogen, and as one of the most effective agents in preventing skin allograft rejection in model systems. LCA is also used to purify numerous glycoproteins (including immunoglobulins, histocompatibility antigens, a2-macroglobulin, etc.) as well as to fractionate glycopeptides from a variety of glycoproteins.||Applications: |Suitable for use in ELISA. Other applications not tested.||Recommended Dilutions:|Optimal dilutions to be determined by the researcher.||Inhibiting/Eluting Sugar: |200mM a-methyl mannoside/200mM a-methyl glucoside mixture||Storage and Stability:|Lyophilized and reconstituted products are stable for 6 months after receipt at -20°C. Reconstitute with sterile 10mM HEPES buffered saline, pH 8.5, 0.1mM Ca++. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.