Human IL-22BP Biotinylated Antibody

Catalog # Availability Size / Price Qty
BAF1087
Product Details
Citations (2)
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Human IL-22BP Biotinylated Antibody Summary

Species Reactivity
Human
Specificity
Detects human IL-22BP in Western blots. In this format, approximately 5% cross-reactivity with recombinant human IL-22 R is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant human IL‑22BP
Thr22-Pro231
Accession # NP_851826
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Label
Biotin

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Human IL‑22BP Fc Chimera (Catalog # 1087-BP)

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.

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Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
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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.
  • 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-22BP

Interleukin 22 binding protein (IL-22BP), also known as cytokine receptor family (CRF) 2‑10, CRF2-X, and IL-22 RA2, is a secreted glycoprotein belonging to the type II cytokine receptor family. The IL-22BP gene has been localized to chromosome 6 near the gene for IFN-gamma R1. It encodes a precursor protein of 231 amino acid (aa) residues with a 21 aa putative signal peptide and five potential N-linked glycolsylation sites. IL-22BP lacks a transmembrane and cytoplasmic domain and is most closely related to the extracellular domains of IL‑22 R (CRF2-9) and IL-20 R (CRF2-8), sharing 33% and 34% aa sequence identity, respectively. It also shares sequence homology with the extracellular domains of IL-10 R (29%), IL-10 R beta (30%), the IFN receptors (23‑25%) and tissue factor (26%). IL-22BP antagonizes IL-22 activity by specifically binding IL-22 with high affinity and blocking its interaction with the cell surface IL-22 receptor heteromeric complex composed IL-22 R and IL‑20 R. IL-22BP is expressed in multiple tissues. The highest levels of expression are found in breast, lungs and colon.

References
  1. Dumoutier, L. et al. (2001) J. Immunol. 166:7090.
  2. Xu, W. et al. (2001) Proc. Natl. Acad. Sci. USA 98:9511.
  3. Kotenko, S. et al. (2001) J. Immunol. 166:7096.
Long Name
Interleukin 22 Binding Protein
Entrez Gene IDs
116379 (Human); 237310 (Mouse)
Alternate Names
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

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Citations for Human IL-22BP Biotinylated 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.

2 Citations: Showing 1 - 2
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  1. Long Interleukin-22 Binding Protein Isoform-1 Is an Intracellular Activator of the Unfolded Protein Response
    Authors: Paloma Gómez-Fernández, Andoni Urtasun, Adrienne W. Paton, James C. Paton, Francisco Borrego, Devin Dersh et al.
    Frontiers in Immunology
  2. The Rare IL22RA2 Signal Peptide Coding Variant rs28385692 Decreases Secretion of IL-22BP Isoform-1, -2 and -3 and Is Associated with Risk for Multiple Sclerosis
    Authors: P Gómez-Fern, A Lopez de L, I Astobiza, J Mena, A Urtasun, V Altmann, F Matesanz, D Otaegui, E Urcelay, A Antigüedad, S Malhotra, X Montalban, T Castillo-T, L Espino-Pai, O Aktas, M Buttmann, A Chan, B Fontaine, PA Gourraud, M Hecker, S Hoffjan, C Kubisch, T Kümpfel, F Luessi, UK Zettl, F Zipp, I Alloza, M Comabella, CM Lill, K Vandenbroe
    Cells, 2020-01-10;9(1):.

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