Human Dermatopontin Antibody

Dermatopontin, also known as TRAMP (tyrosine rich acidic matrix protein), is a widely expressed noncollagenous protein component of the extracellular matrix (1, 2). Mature human Dermatopontin shares 96%, 92%, and 92% amino acid sequence identity with bovine, mouse, and rat Dermatopontin, respectively. It is a 22 kDa molecule that is tyrosine sulfated but not glycosylated (3, 4). Dermatopontin contains three disulfide bonded loop structures that enclose conserved hexapeptide motifs (5). It accelerates collagen fibril formation in vitro, and Dermatopontin deficient mice exhibit altered collagen matrix deposition and organization (6 - 8). Dermatopontin is downregulated in fibrotic growths such as leiomyoma and scar tissue (9, 10). It binds both TGF-beta and the proteoglycan decorin, interactions that can increase the bioavailability of TGF-beta (11, 12). Dermatopontin promotes bone mineralization under the control of the vitamin D receptor and inhibits BMP-2 effects on osteoblast precursors (13, 14).