>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
<1.0 EU per 1 μg of the protein by the LAL method.
Measured by its ability to inhibit IL-10-dependent proliferation of MC/9‑2 mouse mast cells. Thompson-Snipes, L. et al. (1991) J. Exp. Med. 173:507. Approximately 0.1-0.3 µg/mL of IL-10 sR alpha will inhibit 50% of the biological response due to 2 ng/mL of recombinant human IL-10.
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human IL-10 R alpha protein His22-Asn235 Accession # Q13651
Formulation Lyophilized from a 0.2 μm filtered solution in Na HCO3 with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
Background: IL-10 R alpha
Interleukin-10 Receptor alpha (IL‑10 R alpha ), also known as IL‑10 R1, is a 90‑110 kDa transmembrane glycoprotein member of the class II cytokine receptor family (1). IL‑10 R alpha is required for mediating the effects of IL‑10, a critical molecule in the control of microbial infections and allergic and autoimmune inflammation (2‑5). Whereas human IL‑10 is active on mouse cells, mouse IL‑10 does not act on human cells (6). IL‑10 R alpha is the ligand specific subunit of the IL‑10 receptor complex. Noncovalent dimers of IL‑10 bind to IL‑10 R alpha, resulting in the recruitment of IL‑10 R beta (6‑8). IL‑10 R beta is a ubiquitously expressed transmembrane protein that does not bind IL‑10 by itself but is required for signal transduction and in vivo IL‑10 responsiveness (7, 9). IL‑10 R beta also associates with IL‑20 R alpha, IL‑22 R alpha, or IL‑28 R alpha to form the receptor complexes for IL‑22, IL‑26, IL‑28, and IL‑29 (1). Immunosuppressive signal transduction through the IL‑10 receptor complex can be inhibited by activation of TLR2, 4, or 9, enabling strengthened immune responses during infection (10). Some polymorphisms of human IL‑10 R alpha may limit viral immune evasion by retaining full responsiveness to human IL‑10 but responding weakly to the cytomegalovirus homolog of IL‑10 (11). Mature human IL‑10 R alpha consists of a 214 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 322 aa cytoplasmic domain (12). Within the ECD, human IL‑10 R alpha shares 59% aa sequence identity with mouse and rat IL‑10 R alpha.
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