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S100 Calcium Binding Protein A13, Recombinant, Mouse (S100A13)

Cat no: S0052-17K1

S100 Calcium Binding Protein A13, Recombinant, Mouse (S100A13)

Mouse S100A13 is an 11kD member of the S100 (soluble in 100% saturated ammonium sulfate) family of vertebrate EF-hand Ca ++ -binding proteins. It is widely expressed as a homodimer with 98 amino acid (aa) long subunits. Mouse S100A13 shares 87%, 83%, 91%, 86%, 81% and 53% aa identity with rat, human, cow, dog, 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. Some S100 proteins, including S100A13, are able to bind the cell surface receptor for advanced glycation end-products (RAGE). \n\nDespite 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. Binding of copper is necessary for formation of a multi-protein complex between S100A13, FGF-1 and p40 synaptotagmin-1 (syt-1). Cu ++ ions supplied by S100A13 are thought to oxidize and downregulate the activity of FGF-1 prior to export. Calcium influx may also play a similar role in FGF-1 release from neuronal cells. 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 S100A13 has been proposed as a marker for angiogenesis in tumors and endometrium, due to its role in stress-induced export of FGF-1. Based on in house studies, S100A13 has also been found to promote neurite outgrowth from rat cortical embryonic neurons. \n \nMolecular Mass: The non-methionyl form of recombinant mouse S100A13 contains 97 amino acid residues and has a predicted molecular mass of approximately 11kD. \n\nEndotoxin Level: (same/less than) 1EU/ug of the protein as determined by the LAL method. \n\nBiological Activity: Measured by its ability to enhance neurite outgrowth of cortical neurons from E18 rat embryos. Immobilized rmS100A13 (at a 3il droplet containing 50 ng) on a nitrocellulose coated microplate is sufficient to significantly enhance neurite outgrowth. \n\nStorage and Stability:\n\nLyophilized powder may be stored at -20 degrees C. Reconstitute to nominal volume by adding sterile PBS. Aliquot and store at -20 degrees C. Reconstituted product is stable for 1 month at 4 degrees C and 3 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

S0052-17K1

Size

50ug

Reactivities

Mouse

Form

Supplied as a lyophilized powder in PBS. Reconstitute with sterile PBS to a concentration of >100ug/ml . For long term storage a carrier protein (e.g. 0.1% HSA or BSA) should be added.

Purity

> 97%, as determined by SDS-PAGE and visualized by silver stain.

References

1. Santamaria-Kisiel, L. et al. (2006) Biochem. J. 396:201. 9. Prudovsky, I. et al. (2002) J. Cell Biol. 158:201. \n2. Wicki, R. et al. (1996) Biochem. Biophys. Res. Commun. 227:594. 10. Landriscina, M. et al. (2001) J. Biol. Chem. 276:25549. \n3. Ridinger, K. et al. (2000) J. Biol. Chem. 275:8686. 11. Matsunaga, H. & H. Ueda (2006) Cell. Mol. Neurobiol. 26:237. \n4. Li, M. et al. (2007) Biochem. Biophys. Res. Commun. 356:616. 12. Graziani, I. et al. (2006) Biochem. Biophys. Res. Commun. 349:192. \n5. Hsieh, H.-L. et al. (2004) Biochem. Biophys. Res. Commun. 316:949. 13. Landriscina, M. et al. (2006) J. Neurooncol. 80:251. \n6. Landriscina, M. et al. (2001) J. Biol. Chem. 276:22544. 14. Hayrabedyan, S. et al. (2005) Reprod. Biol. 5:51. \n7. Sivaraja, V. et al. (2006) Biophys. J. 91:1832. 15. R&D Sytems (2007) In-house data. \n8. Mandinova, A. et al. (2003) J. Cell Sci. 116:2687.

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