Recombinant Human S100A8/S100A9 Heterodimer (Catalog # 8226-S8) induces IL-6 secretion by A375 human melanoma cells. The ED50 for this effect is 1.5-6 μg/mL.
Background: S100A8/S100A9 Heterodimer
S100A8 (also known as MRP8, Calgranulin A, and CP-10) and S100A9 (also known as MRP14 and Calgranulin B) are pro-inflammatory members of the S100 family of secreted calcium binding proteins (1, 2). They are up-regulated in neutrophils and monocytes at sites of inflammation (e.g. psoriasis, rheumatoid arthritis, cardiac ischemia) and are present at elevated concentrations in rheumatoid arthritis synovial fluid (3-5). The 10 kDa human S100A8 and 14 kDa S100A9 each contain two EF‑hand calcium binding motifs. Human S100A8 shares 57% and 61% amino acid (aa) sequence identity with mouse and rat S100A8, respectively. Human S100A9 shares 57% and 62% amino acid sequence identity with mouse and rat S100A9, respectively (6, 7). S100A8
and S100A9 are noncovalent homodimers that can also noncovalently
heterodimerize; in the presence of calcium and zinc, the homodimer and heterodimers will form tetramers (8-10). The heterodimer additionally binds and sequesters manganese, thereby restricting the growth of Mn-dependent bacteria (11). The S100A8/A9 heterodimer exhibits functions beyond those performed by the individual proteins. These include binding to fatty acids such as arachidonic acid and promoting astrocyte proliferation (3, 12). S100A8, S100A9, and the heterodimer each promote neutrophil infiltration into sites of inflammation and inflammatory cytokine production by monocytes (4, 5, 9).
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S100 Calcium Binding Protein A8/S100 Calcium Binding Protein A9
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