Interleukin 22R, Recombinant, Human (IL-22R, CRF2

IL-22 receptor, also known as IL-22Ra1 and CRF2-9, is an approximately 65 kD transmembrane glycoprotein in the type II cytokine receptor family (CRF). IL-22R contains a 211 aa extracellular domain (ECD) with two fibronectin type III repeats, and a 323 aa cytoplasmic domain. IL-22R associates with either IL-10Rb or IL-20Rb to form receptor complexes with distinct ligand selectivities. IL-10Rb is a shared subunit of the IL-10, -22, -26, -28, and -29 receptors, while IL-20Rb is a shared subunit of the IL-19, -20, -22R and -24 receptors. 1 IL-22R/IL-10 Rb is an IL-22 responsive receptor 2, 3 , and IL-22R/IL-20Rb is an IL-20 or IL-24 responsive receptor. 4, 5 IL-22R contains cytoplasmic motifs for interactions with signal transduction molecules, but formation of ternary complexes with IL-10Rb or IL-20Rb and the respective ligands is required for signal transduction. 2, 6 IL-22BP functions as a competitive antagonist by binding IL-22 and preventing its association with IL-22R. 7, 9 Even though it is a receptor for interleukins, IL-22R is not expressed on hematopoietic cells. 6, 10, 11 Instead, IL-22R expression is restricted to epithelial and stromal cells. 6, 10-13 IL-22R signaling promotes innate immune responses and wound healing at sites of infection and inflammation. This includes upregulation of antimicrobial, acute phase, proinflammatory, and extracellular matrix proteins as well as proteases. 3, 11, 13, 14 IL-22R signaling also promotes downregulation of proteins involved in keratinocyte differentiation. 3, 14 Within the ECD, human IL-22R shares 78%, 76%, and 83% aa sequence identity with mouse, rat, and canine IL-22R, respectively. It shares 22%-25% aa sequence identity with the ECDs of other class II receptors IL-10R, IL-20R, and IL-28R.\n\nSource: Human CD33 Signal Peptide (Met 1-Ala 16), Human IL-22R (Pro 18-Thr 228), HHHHHH; A DNA sequence encoding the signal peptide of human CD33 joined with the extracellular domain of human IL-22R (Pro 18-Thr 228; Accession # NP_067081) (Kotenkok, S.V. et. al., 2001, J. Biol. Chem. 276: 2725-2732) was fused to 6 Histidines at the carboxy terminus. The protein was expressed in a mouse myeloma cell line, NS0.\n\nMolecular Mass: Based on N-terminal amino acid sequencing, the recombinant human IL-22R starts at Pro 18. It has a calculated molecular mass of 24.9 kD. As a result of glycosylation, the recombinant monomer migrates as an approximately 34-38 kD protein in SDS-PAGE under reducing conditions.\n\nEndotoxin Level: < 1.0 EU per 1 microg of the protein as determined by the LAL method.\n\nActivity: Measured by its ability to inhibit rhIL-22-induced IL-10 production by colo 205 cells. The ED50 for this effect is typically 1-4ug/ml in the presence of 1 ng/mL of rhIL-22.\n\nReconstitution: It is recommended that sterile PBS be added to the vial to prepare a working stock solution of no less than 100ug/ml. The carrier-free protein should be used immediately upon reconstitution to avoid losses in activity due to non-specific binding to the inside surface of the vial. For long term storage as a dilute solution, a carrier protein (e.g.\n0.1% HSA or BSA) should be added to the vial.\n\nStorage and Stability: Lyophilized samples are stable for up to twelve months from date of receipt at -20 degrees C. Upon reconstitution, this protein, in the presence of a carrier protein, can be stored under sterile conditions at 2 degrees -8 degrees C for one month or at -20 degrees C in a manual defrost freezer for three months without detectable loss of activity. Avoid repeated freeze-thaw cycles.

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SPECIFICATIONS

Catalog Number

I8443-10H

Size

50ug

Form

Supplied as a lyophilized powder in PBS.

Purity

(same/more than) 95%, as determined by SDS-PAGE and visualized by silver stain.

References

1. Langer, J.A. et al., 2004, Cytokine Growth Factor Rev. 15:33. \n2. Xie, M.-H. et al., 2000, J. Biol. Chem. 275:31335. \n3. Boniface, K. et al., 2005, J. Immunol. 174:3695. \n4. Dumoutier, L. et al., 2001, J. Immunol. 167:3545. \n5. Wang, M. et al., 2002, J. Biol. Chem. 277:7341. \n6. Kotenko, S.V. et al., 2001, J. Biol. Chem. 276:2725. \n7. Li, J. et al., 2004, Int. Immunopharmacol. 4:693. \n8. Logsdon, N.J. et al., 2002, J. Interferon Cytokine Res. 22:1099. \n9. Kotenko, S.V. et al., 2001, J. Immunol. 166:7096. \n10. Nagalakshmi, M.L. et al., 2004, Int. Immunopharmacol. 4:577. \n11. Nagalakshmi, M.L. et al., 2004, Int. Immunopharmacol. 4:679. \n12. Aggarwal, S. et al., 2001, J. Interferon Cytokine Res. 21:1047. \n13. Wolk, K. et al., 2004, Immunity 21:241. \n14. Wolk, K. et al., 2006, Eur. J. Immunol. 36:1309.