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Anti-Glycosaminoglycan Antibody, skin specific Antibody, clone PG-4 clone PG-4, from mouse

ITEM#: 3042-MABT81925UL

MFR#: MABT819-25UL

Proteoglycans (PG), present in all tissues, are one of the best-studied classes of matrix molecules. Over 50 members of PG have been characterized and studied for their biological significance. PG consist of a protein core to which glycosaminoglycan

Proteoglycans (PG), present in all tissues, are one of the best-studied classes of matrix molecules. Over 50 members of PG have been characterized and studied for their biological significance. PG consist of a protein core to which glycosaminoglycan chains are covalently linked. Glycosaminoglycans (GAGs) are natural heteropolysaccharides that are present in every mammalian tissue. They are composed of repeating disaccharide units that consist of either sulfated or non-sulfated monosaccharides. Their molecular size and the sulfation type vary based on tissue type. The major types of GAGs found in mammalian tissues are: hyaluronan, chondroitin sulfate, and dermatan sulfate, heparin and heparan sulfate, and keratan sulfate. GAG chains are covalently bound to serine residues of the PG protein core via a tetrasaccharide linkage, consisting of xylose, two galactose residues and glucuronic acid. This antibody, clone PG-4, recognizes antigen that is associated with extracellular matrices and surfaces of cultured human dermal fibroblasts and the surfaces of cultured human adult keratinocytes. This antibody recognize native epitopes located within glycosaminoglycan chains and is detects both chondroitin sulfate (Versican) and dermatan sulfate (Decorin and Biglycan) proteoglycans. Treatment of PG with chondroitinases is reported to abolish its immunoreactivity for all antigens. (Ref.: Afratis, N et al. (2012). FEBS Journal 279 (7); 1177-1197; Sorrell, JM et al. (1999). Histochem. J. 31 (8); 549-558).