Recombinant Human IL-10 R alpha Fc Avi-tag Protein, CF Summary
Measured by its binding ability in a functional ELISA. When Recombinant Human IL-10 (Catalog # 217-IL/CF or Catalog # 217-ILB/CF) is coated at 2 µg/mL (100 μL/well), Biotinylated Recombinant Human IL‑10 R alpha Fc Chimera Avi-tag binds with an ED50 of 20-100 ng/mL 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. The ED50 for this effect is 6‑48 ng/mL.
|Human IL-10 R alpha |
Accession # Q13651.2
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|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.
When Recombinant Human IL-10 (217-ILB/CF) is coated at 2 μg/mL (100 μL/well), Biotinylated Recombinant Human IL-10 R alpha Fc Chimera Avi-tag (Catalog # AVI9044) binds with an ED50 of 20-100 ng/mL.
2 μg/lane of Biotinylated Recombinant Human IL-10 R alpha Fc Chimera Avi-tag (Catalog # AVI9044) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 74-85 kDa and 148-170 kDa.
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, allergic and autoimmune inflammation, and cancer (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). 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.
- Pestka, S. et al. (2004) Annu. Rev. Immunol. 22:929.
- Manzanillo, P. et al. (2015) Trends Immunol. 36:471.
- Sziksz, E. et al. (2015) Mediators Inflamm. 2015:764641.
- Mannino, M.H. et al. (2015) Cancer Lett. 367:103.
- Fitzgerald, D.C. et al. (2007) Nat. Immunol. 8:1372.
- Tan, J.C. et al. (1993) J. Biol. Chem. 268:21053.
- Kotenko, S.V. et al. (1997) EMBO J. 16:5894.
- Tan, J.C. et al. (1995) J. Biol. Chem. 270:12906.
- Spencer, S.D. et al. (1998) J. Exp. Med. 187:571.
- Fernandez, S. et al. (2004) J. Immunol. 172:2613.
- Gruber, S.G. et al. (2008) Eur. J. Immunol. 38:3365.
- Liu, Y. et al. (1994) J. Immunol. 152:1821.
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