Human Chemerin Antibody

Human Chemerin, also known as Tazarotene-induced Gene 2, (TIG2) is a new, but distant member of the Cystatin superfamily (1 - 3). Members of this superfamily contain at least two intrachain disulfide bonds and an alpha-helical structure over a distance of about 100 amino acids (2, 3). Chemerin is synthesized as a 163 aa precursor that contains a hydrophobic 20 aa N-terminal sequence, an intervening 137 aa Cystatin-fold containing domain, and a six aa C-terminal prosegment (1, 4). Within the cystatin-fold domain there are three intrachain disulfide bonds that contribute to the fold, and three potential sites for phosphorylation and one for myristoylation (5). The precursor molecule undergoes proteolytic processing at both termini by unknown proteases. The N-terminal residue 20 aa hydrophobic segment is described as being either a signal sequence or a transmembrane (TM) segment for a type II TM protein (1, 6). In either case, it gives rise to a soluble proform that undergoes further processing at the C-terminus. In human, the C-terminal six residues are cleaved, giving rise to a monomeric, 16 kDa heparin-binding bioactive molecule (aa 21 - 157) (7). A shorter 134 aa form has been described (5). Bioactivity seems to be concentrated in the nine residues preceding the prosegment (aa 149 ‑ 157). Retention of the prosegment blocks activity (4). The 137 aa mature segment is known to bind to the G-protein coupled receptor termed ChemR23 (5, 7). Binding results in macrophage and immature dendritic cell chemotaxis (7). The distribution of this receptor is limited to immune APCs, and it is assumed that Chemerin is an inflammatory molecule. It is unclear which cells are actually producing Chemerin, but keratinocytes, endothelial cells and osteoclasts are potential candidates (1, 7). Mature human Chemerin shares 67% aa sequence identity with mouse Chemerin (7). There is apparently cross-species activity for the protein (8).