Recombinant Human S100A8 Protein, CF Summary
|Formulation||Lyophilized from a 0.2 μm filtered solution in Tris and TCEP with Trehalose.|
|Reconstitution||Reconstitute at 150 μg/mL in water.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||
Recombinant Human S100A8 (Catalog # 9876-S8) induces CXCL1/KC secretion in C3H10T1/2 mouse embryonic fibroblast cells. The ED50 for this effect is 4-20 μg/mL.
S100A8 (also known as MRP8 and calgranulin A) is a 10 kDa member of the S100 family, EF-hand superfamily of Ca2+ binding proteins (1, 2). It is produced by neutrophils and monocytes, and forms Ca2+ dependent heterodimer/ heterotetramer complexes (termed calprotectin) with S100A9 in addition to forming homodimeric complexes. Like S100A9, S100A8 is up-regulated in neutrophils and monocytes at sites of inflammation (e.g. psoriasis, rheumatoid arthritis, cardiac ischemia) and is present at elevated concentrations in rheumatoid arthritis synovial fluid (3-5). It functions both intracellularly and extracellularly, where it binds to RAGE and CD36. In addition, S100A8 was shown to activate lung alveolar epithelial cells, osteoclasts, and chondrocytes in TLR4-dependent manner, inducing proinflammatory cytokines and chemokines including, IL-6, IL-8, KC, and MCP-1 (6-8). In osteoarthritic chondrocytes, S100A8 and A9 also promoted expression of matrix metalloproteinases (MMP-1, -3, -9, and -13) potentially affecting to cartilage breakdown (8). Human S100A8 is 93 amino acids (aa) in length. It contains two EF-hand motifs (aa 12-47 and aa 46-81) and one high-affinity Ca2+ binding site (aa 59-70). There may be one splice form that shows a 15 aa substitution for the C-terminal 14 amino acids. Although mouse S100A8 is cleaved by MMP‑2 after Asn21, it is unclear if human S100A8 is susceptible to the same cleavage. Full-length human S100A8 is 57% and 61% identical to mouse and rat S100A8, respectively (9).
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- Vogl, T. et al. (2012) Int. J. Mol. Sci. 13:2893
- Siegenthaler, G. et al. (1997) J. Biol. Chem. 272:9371.
- Sunahori, K. et al. (2006) Arthritis Res. Ther. 8:R69.
- Volz, H.C. et al. (2012) Basic Res. Cardiol. 107:250
- Chakraborty D. et al. (2017) Front Immunol. 8:1493
- Grevers L.C. Arthritis Rheum. 63:1365
- Schelbergen R.F. Arthritis Rheum. 64:1477
- Odink, K. et al. (1987) Nature 330:80
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