Galectin-4, His Tag, human recombinant (rHuGAL4-His)

Galectin that binds lactose and a related range of sugars. May be involved in the assembly of adherens junctions. (www.uniprot.org) Human recombinant Galectin-4 produced in E.coli is a single, non-glycosylated, polypeptide chain containing 343 amino acids (fragment 1-323) and having a molecular mass of 38.1kDa. Galectin-4 is fused to 20 amino acid His-Tag at N-terminus. Galectin-4 is a member of the subfamily of galectins composed of two carbohydrate recognition domains having similar peptide chains. The galectins are a family of beta-galactoside-binding proteins having a role in modulating cell-cell and cell-matrix interactions, which inhibits chronic inflammations, GVHD, and allergic responses. LGALS4 expression is limited to small intestine, colon, and rectum, and it is underexpressed in colorectal cancer. LGALS4 binds as an endogenous ligand to glycosphingolipids having 3-O-sulfated Gal residues and bind as well to cholesterol-3-sulfate. LGALS4 takes part in cell adhesion. LGALS4 plays a role in crosslinking the lateral cell membranes of the surface-lining epithelial cells, thus supporting epithelial integrity against mechanical stress exerted by the bowel lume. LGALS4 is in charge of intestinal inflammation via selective regulation of peripheral and mucosal T-cell cell cycle, in addition to cell death by apoptosis of T-cells by a pathway independent of the activation of caspases. LGALS4 blockade decreases TNF-alpha inhibitor induced T-cell death. LGALS4 decreases pro-inflammatory cytokine secretion including IL-6 and IL-17.