Recombinant Human IL-22BP Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit IL-22-induced IL-10 secretion by COLO 205 human colorectal adenocarcinoma cells. The ED50 for this effect is 4-20 ng/mL in the presence of 1 ng/mL of Recombinant Human IL-22 (Catalog # 782-IL).
Source
Mouse myeloma cell line, NS0-derived human IL-22BP protein
Human IL-22BP (Thr22-Pro231) Accession # NP_851826
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
51.3 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
75-80 kDa, reducing conditions
Publications
Read Publications using 1087-BP in the following applications:
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human IL-22BP Fc Chimera Protein, CF
class II cytokine receptor
CRF2-10
CRF2-S1IL22BP
CRF2-X
Cytokine receptor class-II member 10
Cytokine receptor family 2 member 10
Cytokine receptor family type 2, soluble 1
IL-22 RA2
IL-22 receptor subunit alpha-2
IL22BP
IL-22BP
IL-22BPCRF2X
IL22RA2
IL-22RA2
IL-22R-alpha-2
interleukin 22 receptor, alpha 2
interleukin 22-binding protein
interleukin-22 receptor subunit alpha-2
Interleukin-22-binding protein
MGC150509
MGC150510
zcytoR16
Background
Interleukin 22 binding protein (IL-22BP), also known as CRF2-10, CRF2-X, and IL-22 RA2, is a 35-45 kDa secreted glycoprotein in the type II cytokine receptor family (CRF). IL-22 signals through a receptor complex consisting of IL-22 R and IL-10 R beta . IL-10 R beta is also a component of the receptor complexes for IL-10, IL-26, IL-28, and IL-29 (1, 2). IL-22BP blocks the interaction of IL-22 with IL-22 R, preventing IL-22 induced production of reactive oxygen species, IL-6, IL-10, and TNF-a (3-8). In vivo, it regulates the proinflammatory effects of IL-22 (e.g. neutrophil infiltration) but not of IL-10 (7). Mouse IL-22BP can neutralize the bioactivity of both mouse and human IL-22 (6). IL-22BP is produced by dendritic cells (DC), epithelial cells, activated B cells, and activated monocytes (3, 6, 9, 10). It is constitutively expressed by DC but is down-regulated during local inflammation and in response to tissue damage (11-13). IL-22BP is critical for limiting IL-22 induced epithelial cell proliferation during wound healing, and its deficiency can enable uncontrolled proliferation and enhance tumor development (12). Mature human IL-22BP contains two Fibronectin type-III domains (4, 6). Alternative splicing generates additional isoforms that contain a 32 amino acid (aa) insertion in the first Fn-III domain and may also be truncated within the second Fn-III domain (3, 4, 14). Human IL-22BP without the 32 aa insertion shares 68% and 73% amino acid (aa) sequence identity with mouse and rat IL-22BP, respectively.
Lim, C. and R. Savan (2014) Cytokine Growth Factor Rev. 25:257.
Mizoguchi, A. (2012) Inflamm. Bowel Dis. 18:1777.
Xu, W. et al. (2001) Proc. Natl. Acad. Sci. USA 98:9511.
Kotenko, S.V. et al. (2001) J. Immunol. 166:7096.
Li, J. et al. (2004) Int. Immunopharmacol. 4:693.
Wei, C.-C. et al. (2003) Genes Immun. 4:204.
Weber, G.F. et al. (2007) Infect. Immun. 75:1690.
Whittington, H.A. et al. (2004) Am. J. Respir. Cell Mol. Biol. 31:220.
Lecart, S. et al. (2002) Int. Immunol. 14:1351.
Nagalakshmi, M.L. et al. (2004) Int. Immunopharmacol. 4:577.
Wolk, K. et al. (2007) J. Immunol. 178:5973.
Huber, S. et al. (2012) Nature 491:259.
Martin, J.C.J. et al. (2014) Mucosal Immunol. 7:101.
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