Recombinant Human S100A1 Protein, CF

When Recombinant Human S100A1 (Catalog # 9705‑S1) is coated at 1 μg/mL, recombinant human HSP70/HSPA1A binds with an ED50 of 0.8‑4.8 μg/mL.

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

Recombinant Human S100A1 Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human S100A1 is immobilize at 1 μg/mL, 100 μL/well, it binds recombinant human HSP70/HSPA1A. The concentration of recombinant human HSP70/HSPA1A that produces 50% of the optimal binding response is 0.8-4.8 μg/mL.
• Source: E. coli-derived human S100A1 protein
  Met1-Ser94
• Accession #: P23297
• N-terminal Sequence: Met1 & Gly2
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 11 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.
• SDS-PAGE: 7 kDa, reducing conditions

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 and DTT.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 1 mg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human S100A1 Protein, CF

• protein S100-A1
• S100 alpha
• S100 calcium binding protein A1
• S100 calcium-binding protein A1S100
• S-100 protein alpha chain
• S-100 protein subunit alpha
• S100 protein, alpha polypeptide
• S100A
• S100A1
• S100-alpha

Background

S100A1, also known as S100 Alpha, is a 10 kDa member of the S100 (soluble in 100% ammonium sulfate at neutral pH) family of proteins (1-5). The S100 family is further classified as a member of the EF-hand superfamily of Ca2⁺ binding protein. The hallmark of this superfamily is the EF-hand motif that consists of a Ca2⁺‑binding site flanked by two alpha -helices (helix E and helix F) that were originally identified in a right-handed model of carp muscle calcium-binding protein (6). S100A1 can also bind zinc in vitro and its binding sites are different from the calcium binding sites. Typically, S100A1 exists as homodimers but it can also form non-covalent heterodimers with other members of the S100 family (7, 8). Human S100A1 is 94 amino acids (aa) in length. It shares 93%, 94%, 98% and 100% aa sequence identity with mouse, rat, bovine and Rhesus macaque respectively (9). Within the S100 family, S100A1 shows the highest aa identity (56%) with S100B (10). S100 A1 is highly expressed in the myocardium, and it is an important regulator of the cardiac contractility (11, 12). S100A1 acts as a Ca2⁺ signal transducer (13). In response to an increase in intracellular Ca2⁺ levels, S100 A1 binds calcium which triggers a conformational change (14). This conformational change allows interaction of S100A1 with specific target proteins, such as TPR-containing proteins, and the modulation of their activity (13). S100A1 also acts as a cardioprotective factor to inhibit apoptosis in neonatal ventricular cardiomyocytes via activation of the ERK1/2 (12).

1. Engelkamp, D. et al. (1992) Biochemistry 31:10258.
2. Tomida, Y. et al. (1992) Biochem. Biophys. Res. Commun. 189:1310.
3. Garrett, S.C. et al. (2006) J. Biol. Chem. 281:677.
4. Santamaria-Kisiel, L. et al. (2006) Biochem. J. 396:201.
5. Donato, R. (2001) Int. J. Biochem. Cell. Biol. 33:637.
6. Kretsinger, R.H. and C.E. Nockolds (1973) J. Biol. Chem. 248:3313.
7. Wang, G. et al. (2004) Biochem. J. 382:375.
8. Wang, G. et al. (2000) J. Biol. Chem. 275:11141.
9. Ridinger, K et al. (1998) Biochem. Biophys. Acta 1448:254.
10. Donato R. et al. (1999) Braz J Med Biol Res. 32(10):1177.
11. Duarte-Costa, S. et al. (2014) Physiol. Res. 63:669
12. Most, P. et al. (2003) J. Biol. Chem. 278:48404.
13. Yamaguchi F. et al. (2012) J. Biol. Chem. 287:13787.
14. Nowakowski M. et al. (2013) Biochemistry 52:1149.

Bioinformatics

• Uniprot:
  • P23297()