Human IL-22 R alpha 1 Antibody Summary
Pro18-Thr228
Accession # Q8N6P7
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
IL‑10 secretion Induced by IL‑22 and Neutralization by Human IL‑22 R alpha 1 Antibody. Recombinant Human IL-22 (Catalog # 782-IL) stimulates IL-10 secretion in the COLO 205 human colorectal adenocarcin-oma cell line in a dose-dependent manner (orange line), as measured by the Human IL-10 DuoSet ELISA Development Kit (Catalog # DY217B). IL-10 secretion elicited by Recombinant Human IL-22 (1 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Human IL-22 Ra1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2770). The ND50 is typically 0.2-1 µg/mL.
Detection of Human IL-22R alpha 1 by Flow Cytometry Stimulation of AGS cells with IL-22 leads to the inhibition of H. pylori-induced CCL20 expression.A, AGS cells were stained with an isotype control antibody (dashed line) or an anti-IL-22R1 antibody (solid line) conjugated with allophycocyanin and analyzed by flow cytometry. B, AGS cells were infected with H. pylori (HP) in the presence of various concentration of IL-22 for 24 h and the CCL20 concentration in the culture supernatants was determined by ELISA. C-D, AGS cells were infected with H. pylori in the presence or absence of IL-22 and the CCL20 mRNA in the cells (C) and CCL20 protein in the culture supernatants (D) were determined by real-time PCR and ELISA, respectively. E. AGS cells were pretreated with a neutralizing antibody against IL-22R1 (2 µg/ml) for 1 h followed by the H. pylori infection in the absence or presence of IL-22 for 6 h. The CCL20 concentration in the culture supernatants was determined by ELISA. Data represent the mean ± SEM from three independent experiments. **, p<0.005; *, p<0.02 for H. pylori + IL-22 versus H. pylori only. Image collected and cropped by CiteAb from the following publication (https://dx.plos.org/10.1371/journal.pone.0097350), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of Human IL-22R alpha 1 by Western Blot IL-22 and IL-22 receptor expression levels increase in the airways of asthmatic subjects. (A-D) Bronchial biopsies were obtained from healthy controls, mild asthmatics and severe asthmatics and stained (A, negative control) for IL-22 expression (in brown) by immunohistochemistry. Scale bar 50 μm. (E) The number of IL-22 positive cells was determined per mm2 of biopsy tissue. n=5 per group, *p<0.05 vs. healthy control. (F) Primary bronchial epithelial cells were obtained from healthy controls, mild asthmatics and severe asthmatics and assessed for IL-22 receptor expression by Western blot. Cells were allowed to grow to confluence, serum starved overnight and stimulated with IL-22, TGF-beta 1 (10 ng/mL each) or both cytokines for 5 days before Western blot analysis. (G) Expression levels of the IL-22 receptor in unstimulated cells were quantified relative to GAPDH expression. n=5 per group, *p<0.05 vs. healthy control. Image collected and cropped by CiteAb from the following publication (https://respiratory-research.biomedcentral.com/articles/10.1186/1465-9921-14-118), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of Human IL-22R alpha 1 by Immunohistochemistry IL-22 and IL-22 receptor expression levels increase in the airways of asthmatic subjects. (A-D) Bronchial biopsies were obtained from healthy controls, mild asthmatics and severe asthmatics and stained (A, negative control) for IL-22 expression (in brown) by immunohistochemistry. Scale bar 50 μm. (E) The number of IL-22 positive cells was determined per mm2 of biopsy tissue. n=5 per group, *p<0.05 vs. healthy control. (F) Primary bronchial epithelial cells were obtained from healthy controls, mild asthmatics and severe asthmatics and assessed for IL-22 receptor expression by Western blot. Cells were allowed to grow to confluence, serum starved overnight and stimulated with IL-22, TGF-beta 1 (10 ng/mL each) or both cytokines for 5 days before Western blot analysis. (G) Expression levels of the IL-22 receptor in unstimulated cells were quantified relative to GAPDH expression. n=5 per group, *p<0.05 vs. healthy control. Image collected and cropped by CiteAb from the following publication (https://respiratory-research.biomedcentral.com/articles/10.1186/1465-9921-14-118), licensed under a CC-BY license. Not internally tested by R&D Systems.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: IL-22 R alpha 1
IL-22 receptor, also known as IL-22 R alpha 1 and CRF2-9, is an approximately 65 kDa transmembrane glycoprotein in the type II cytokine receptor family (CRF). IL-22 R alpha 1 contains a 211 amino acid (aa) extracellular domain (ECD) with two fibronectin type III repeats, and a 323 aa cytoplasmic domain. IL-22 R alpha 1 associates with either IL-10 R beta or IL-20 R beta to form receptor complexes with distinct ligand selectivities. IL-10 R beta is a shared subunit of the IL-10, -22, -26, -28, and -29 receptors, while IL-20 R beta is a shared subunit of the IL-19, -20, -22R and -24 receptors (1). IL-22 R alpha 1/IL-10 R beta is an IL-22 responsive receptor (2, 3), and IL-22 R alpha 1/IL-20 R beta is an IL-20 or IL-24 responsive receptor (4, 5). IL-22 R alpha 1 contains cytoplasmic motifs for interactions with signal transduction molecules, but formation of ternary complexes with IL-10 R beta or IL-20 R beta 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-22 R alpha 1 (7, 9). Even though it is a receptor for interleukins, IL-22 R alpha 1 is not expressed on hematopoietic cells (6, 10, 11). Instead, IL-22 R alpha 1 expression is restricted to epithelial and stromal cells (6, 10‑13). IL-22 R alpha 1 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-22 R alpha 1 signaling also promotes downregulation of proteins involved in keratinocyte differentiation (3, 14). Within the ECD, human IL-22 R alpha 1 shares 78%, 76%, and 83% aa sequence identity with mouse, rat, and canine IL-22 R, respectively. It shares 22% - 25% aa sequence identity with the ECDs of other class II receptors IL-10 R, IL-20 R, and IL-28 R.
- Langer, J.A. et al. (2004) Cytokine Growth Factor Rev. 15:33.
- Xie, M.-H. et al. (2000) J. Biol. Chem. 275:31335.
- Boniface, K. et al. (2005) J. Immunol. 174:3695.
- Dumoutier, L. et al. (2001) J. Immunol. 167:3545.
- Wang, M. et al. (2002) J. Biol. Chem. 277:7341.
- Kotenko, S.V. et al. (2001) J. Biol. Chem. 276:2725.
- Li, J. et al. (2004) Int. Immunopharmacol. 4:693.
- Logsdon, N.J. et al. (2002) J. Interferon Cytokine Res. 22:1099.
- Kotenko, S.V. et al. (2001) J. Immunol. 166:7096.
- Nagalakshmi, M.L. et al. (2004) Int. Immunopharmacol. 4:577.
- Nagalakshmi, M.L. et al. (2004) Int. Immunopharmacol. 4:679.
- Aggarwal, S. et al. (2001) J. Interferon Cytokine Res. 21:1047.
- Wolk, K. et al. (2004) Immunity 21:241.
- Wolk, K. et al. (2006) Eur. J. Immunol. 36:1309.
Product Datasheets
Citations for Human IL-22 R alpha 1 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 9
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IL-22 expression is increased variedly in the initial phase, onset and chronic phase of a pristane-induced arthritis rat model
Authors: Weikun Hou, Bo Wang, Yan Zhou, Ke Xu, Liesu Meng, Wenhua Zhu et al.
Molecular Medicine Reports
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Interleukin-22 regulates B3GNT7 expression to induce fucosylation of glycoproteins in intestinal epithelial cells
Authors: DJ Carroll, MWN Burns, L Mottram, DC Propheter, A Boucher, GM Lessen, A Kumar, SA Malaker, C Xing, LV Hooper, U Yrlid, JJ Kohler
The Journal of Biological Chemistry, 2021-12-02;0(0):101463.
Species: Human
Sample Types: Organoid
Applications: Neutralization -
IL-22 negatively regulates Helicobacter pylori-induced CCL20 expression in gastric epithelial cells.
Authors: Chen J, Wu M, Kuo S, Liao F
PLoS ONE, 2014-05-13;9(5):e97350.
Species: Human
Sample Types: Whole Cells
Applications: Neutralization -
IL-22 contributes to TGF-beta1-mediated epithelial-mesenchymal transition in asthmatic bronchial epithelial cells.
Authors: Johnson J, Nishioka M, Chakir J, Risse P, Almaghlouth I, Bazarbashi A, Plante S, Martin J, Eidelman D, Hamid Q
Respir Res, 2013-11-01;14(0):118.
Species: Human
Sample Types: Cell Lysates
Applications: Western Blot -
IL-22 suppresses IFN-gamma-mediated lung inflammation in asthmatic patients.
Authors: Pennino D, Bhavsar P, Effner R, Avitabile S, Venn P, Quaranta M, Marzaioli V, Cifuentes L, Durham S, Cavani A, Eyerich K, Chung K, Schmidt-Weber C, Eyerich S
J Allergy Clin Immunol, 2012-11-19;131(2):562-70.
Species: Human
Sample Types: Whole Cells
Applications: Blocking -
IL-17 and IL-22 mediate IL-20 subfamily cytokine production in cultured keratinocytes via increased IL-22 receptor expression.
Authors: Tohyama M, Hanakawa Y, Shirakata Y, Dai X, Yang L, Hirakawa S, Tokumaru S, Okazaki H, Sayama K, Hashimoto K
Eur. J. Immunol., 2009-10-01;39(10):2779-88.
Species: Human
Sample Types: Cell Lysates, Whole Tissue
Applications: IHC-Fr, Western Blot -
Interleukin-22 participates in the inflammatory process of vitiligo
Authors: Jinjin Dong, Xiaohong An, Hui Zhong, Yichuan Wang, Jing Shang, Jia Zhou
Oncotarget
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Interleukin-22 Might Act as a Double-Edged Sword in Type 2 Diabetes and Coronary Artery Disease
Authors: Fangchen Gong, Jin Wu, Ping Zhou, Mengyao Zhang, Jingning Liu, Ying Liu et al.
Mediators of Inflammation
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Crystal structure of the labile complex of interleukin 24 (IL-24) with the extracellular domains of IL-22R1 and IL-20R2
Authors: Jacek Lubkowski, Cem Sonmez, Sergey V. Smirnov, Andriy Anishkin, Sergei V. Kotenko, Alexander Wlodawer
The Journal of Immunology
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We used this antibody in an in-house ELISA along with mAb (2770) and protein standard (2770-LR) to quantify IL-22R alpha1 in human serum and plasma. This combination could not detect IL-22R alpha1 in our samples but generated a good standard curve.