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Recombinant Human IL-22BP Fc Chimera Avi-tag Protein, CF

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Measured by its binding ability in a functional ELISA. When Recombinant Human IL-22 Protein (782-IL) is coated at 0.500 µg/mL (100 µL/well), Biotinylated Recombinant Human IL‑22BP Fc Chimera Avi-tag (Catalog # AVI1087) binds with an ED50 of 50.0-400 ng/mL.
Measured by its binding ability in a functional ELISA. When Recombinant Human IL-22 Protein (782-IL) is coated at 0.500 µg/mL (100 µL/well), Biotinylated Recombinant Human IL‑22BP Fc Chimera Avi-tag (Catalog # ...read more
2 μg/lane of Recombinant Human IL-22BP Fc Chimera Avi-tag Protein (Catalog # AVI1087) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human IL-22BP Fc Chimera Avi-tag Protein, CF Summary

Additional Information
Biotinylated
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human IL-22 Protein (Catalog # 782-IL) is coated at 0.500 µg/mL (100 µL/well), Biotinylated Recombinant Human IL‑22BP Fc Chimera Avi-tag (Catalog # AVI1087) binds with an ED50 of 50.0-400 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human IL-22BP protein
Human IL-22BP
(Thr22-Pro231)
Accession # NP_851826.1		IEGRMDHuman IgG1
(Pro100-Lys330)		Avi-tag
N-terminusC-terminus
N-terminal Sequence
Thr22
Structure / Form
Disulfide-linked homodimer
Biotinylated via Avi-tag
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
53 kDa.
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
73-82 kDa, under reducing conditions.

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

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 Avi-tag 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 CRF210, CRF2X, 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-10Rb. IL-10Rb 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, IL6, IL-10, and TNFa (3-8). In vivo, it regulates the proinflammatory effe-cts 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 acids (aa) insertion in the first FnIII domain and may also be truncated within the second Fc-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. Our Avi-tag Biotinylated Recombinant Human IL‑22BP features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
  1. Lim, C. and R. Savan (2014) Cytokine Growth Factor Rev. 25:257.
  2. Mizoguchi, A. (2012) Inflamm. Bowel Dis. 18:1777.
  3. Xu, W. et al. (2001) Proc. Natl. Acad. Sci. USA 98:9511.
  4. Kotenko, S.V. et al. (2001) J. Immunol. 166:7096.
  5. Li, J. et al. (2004) Int. Immunopharmacol. 4:693.
  6. Wei, C.-C. et al. (2003) Genes Immun. 4:204.
  7. Weber, G.F. et al. (2007) Infect. Immun. 75:1690.
  8. Whittington, H.A. et al. (2004) Am. J. Respir. Cell Mol. Biol. 31:220.
  9. Lecart, S. et al. (2002) Int. Immunol. 14:1351.
  10. Nagalakshmi, M.L. et al. (2004) Int. Immunopharmacol. 4:577.
  11. Wolk, K. et al. (2007) J. Immunol. 178:5973.
  12. Huber, S. et al. (2012) Nature 491:259.
  13. Martin, J.C.J. et al. (2014) Mucosal Immunol. 7:101.
  14. Dumoutier, L. et al. (2001) J. Immunol. 166:7090.

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