Recombinant Human S100A13 Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human S100A13 Protein, CF Summary

• Details of Functionality: Measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons. Able to significantly enhance neurite outgrowth when immobilized as a 3 µL droplet containing 100 ng on a nitrocellulose-coated microplate.
• Source: E. coli-derived human S100A13 protein
  Ala2-Lys98
• Accession #: NP_005970
• N-terminal Sequence: Ala2
• Protein/Peptide Type: Recombinant Proteins
• Gene: S100A13
• Purity: >97%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 11.3 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >97%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile Dulbecco's PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human S100A13 Protein, CF

• S100 calcium binding protein A13
• S100 calcium-binding protein A13protein S100-A13
• S100A13

Background

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).

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

Bioinformatics

• Gene Symbol: S100A13
• Uniprot:
  • NP_005970()