Mouse S100A13 Antibody Summary
Ala2-Lys98
Accession # P97352
Applications
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.
Scientific Data
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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.
Reconstitution Calculator
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.
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).
- Santamaria-Kisiel, L. et al. (2006) Biochem. J. 396:201.
- Wicki, R. et al. (1996) Biochem. Biophys. Res. Commun. 227:594.
- Ridinger, K. et al. (2000) J. Biol. Chem. 275:8686.
- Li, M. et al. (2007) Biochem. Biophys. Res. Commun. 356:616.
- Hsieh, H-L. et al. (2004) Biochem. Biophys. Res. Commun. 316:949.
- Landriscina, M. et al. (2001) J. Biol. Chem. 276:22544.
- Sivaraja, V. et al. (2006) Biophys. J. 91:1832.
- Mandinova, A. et al. (2003) J. Cell Sci. 116:2687.
- Prudovsky, I. et al. (2002) J. Cell Biol. 158:201.
- Landriscina, M. et al. (2001) J. Biol. Chem. 276:25549.
- Matsunaga, H. and H. Ueda (2006) Cell. Mol. Neurobiol. 26:237.
- Graziani, I. et al. (2006) Biochem. Biophys. Res. Commun. 349:192.
- Landriscina, M. et al. (2006) J. Neurooncol. 80:251.
- Hayrabedyan, S. et al. (2005) Reprod. Biol. 5:51.
- R&D Sytems (2007) In-house data.
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