Human S100A13 Antibody

S100A13 is an 11 kDa member of the S100 (soluble in 100% saturated ammonium sulfate) family of vertebrate EF-hand Ca⁺⁺-binding proteins (1‑3). It is widely expressed as a homodimer with two 98 amino acid (aa) long subunits (2, 3). Human S100A13 shares 83%, 90%, 91%, 87%, 78% and 47% aa identity with mouse, rat, cow, dog, opossum and chicken S100A13, respectively. Like other S100 proteins, S100A13 is small and generally acidic, but contains a basic residue-rich sequence at the C terminus, and two EF hand motifs that bind with Ca⁺⁺ differing affinities (2‑4). Some S100 proteins, including S100A13, are able to bind the cell surface receptor for advanced glycation end-products (RAGE) (5). Despite lacking a signal sequence, S100A13 plays an important role in Cu⁺⁺-dependent export of FGF-1 (FGF acidic) and IL-1 alpha from the cell in response to stresses such as heat shock, anoxia and starvation (6‑8). Binding of copper is necessary for formation of a multi-protein complex between S100A13, FGF-1 and p40 synaptotagmin-1 (syt-1) (9, 10). Cu⁺⁺ ions supplied by S100A13 are thought to oxidize and downregulate the activity of FGF-1 prior to export (10). Calcium influx may also play a similar role in FGF-1 release from neuronal cells (11). S100A13 is composed of four amphiphilic helices that may interact with acidic phospholipid headgroups. With FGF-1 and syt-1, S100A13 likely perturbs the membrane, which allows the S100A13 protein complex to exit the cell (4, 12). S100A13 has been proposed as a marker for angiogenesis in tumors and endometrium, due to its role in stress-induced export of FGF-1 (13, 14). Based on in house studies, S100A13 has also been found to promote neurite outgrowth from rat cortical embryonic neurons (15).