Mouse S100A13 Antibody Summary
Accession # P97352
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
S100A13 in Mouse Embryo. S100A13 was detected in immersion fixed frozen sections of mouse embryo using 15 µg/mL Goat Anti-Mouse S100A13 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4328) overnight at 4 °C. Tissue was stained with the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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).
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- R&D Sytems (2007) In-house data.
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