Recombinant Mouse S100A13 Protein, CF

Recombinant Mouse S100A13 Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: S100A13

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 98 amino acid (aa) long subunits (2, 3). Mouse S100A13 shares 87%, 83%, 91%, 86%, 81% and 53% aa identity with rat, human, bovine, canine, opossum and chicken S100A13, respectively. Like other S100 proteins, S100A13 is small and generally acidic, but it contains a basic residue-rich sequence at the C-terminus, and two EF hand motifs that bind Ca⁺⁺ with 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).

Related Research Areas

• Calcium-binding Proteins and Related Molecules
• Inflammatory Mediators