Recombinant Mouse IL-23R Fc Chimera Protein, CF

Catalog # Availability Size / Price Qty
1686-MR-050
Product Details
Citations (2)
FAQs
Supplemental Products
Reviews (1)

Recombinant Mouse IL-23R Fc Chimera Protein, CF Summary

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.1 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its binding ability in a functional ELISA. When Recombinant Mouse IL-23 R/Fc Chimera is immobilized at 5 µg/mL (100 µL/well) the concentration of  Recombinant Mouse IL‑23 (Catalog # 1887-ML) that produces 50% of optimal binding response is approximately 5-25 ng/mL
Source
Mouse myeloma cell line, NS0-derived mouse IL-23 R protein
Mouse IL-23 R
(Gly24-Asp372)
Accession # Q8K4B4
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Analysis
Gly24
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
66.8 kDa (monomer)
SDS-PAGE
105 kDa, reducing conditions

Product Datasheets

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

1686-MR

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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Reconstitution Calculator

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Background: IL-23R

Interleukin 23 (IL-23) is a heterodimeric cytokine composed of two disulfide-linked subunits, a p19 subunit that is unique to IL-23, and a p40 subunit that is shared with IL-12 (1 - 5). The functional IL-23 receptor complex consists of two receptor subunits, the IL-12 receptor beta 1 subunit (IL-12 R beta 1) and the IL-23-specific receptor subunit (IL-23 R) (3). Mouse IL-23 R cDNA encodes a 644 amino acid (aa) type I transmembrane protein with a 23 aa residue signal peptide, a 349 aa residue extracellular domain, a 23 aa residue transmembrane domain and a 249 aa residue cytoplasmic region. IL-23 R shares structural features with the IL-12 R beta 2, including an N-terminal Ig-like domain, two cytokine receptor domains and multiple glycosylation sites in the extracellular domain. IL-23 R lacks the three extracellular membrane-proximal fibronectin-type III domains present on IL-12 R beta 2. IL-23 R has a WQPWS sequence in the transmembrane-proximal cytokine receptor domain similar to the cytokine receptor signature WSXWS motif. The cytoplasmic region of IL-23 R has three potential Src homology 2 domain-binding sites and two potential Stat-binding sites. The gene for human IL-23 R is located on human chromosome 1 within 150 kb of IL-12 R beta 2. Human and mouse IL-23 R share 66% amino acid sequence identity. Mouse IL-23 R is expressed in mouse Th1 and Th2 cells, bone marrow, dendritic cells and macrophages. It is also expressed by mouse CD4+ CD45RBlow memory T cells, but at much lower levels by mouse CD4+ CD45RBhigh cells. IL-23 initiates a signal transduction cascade similar to that of IL-12, and involves Jak2, Tyk2, Stat1, Stat3, Stat4, and Stat5. IL-23 has biological activities that are similar to, but distinct from IL-12.

References
  1. Oppmann, B. et al. (2000) Immunity 13:715.
  2. Lankford, C.S. and D.M. Frucht (2003) J. Leukoc. Biol. 73:49.
  3. Parham, C. et al. (2002) J. Immunol. 168:5448.
  4. Belladonna, M.L. et al. (2002) J. Immunol. 168:5448.
  5. Aggarwal, S. et al. (2003) J. Biol. Chem. 278:1910.
Long Name
Interleukin 23 Receptor
Entrez Gene IDs
149233 (Human); 209590 (Mouse); 102133210 (Cynomolgus Monkey)
Alternate Names
IBD17; IL-23 R; IL-23 receptor; IL23R; IL-23R; interleukin 23 receptor; interleukin-23 receptor

Citations for Recombinant Mouse IL-23R Fc Chimera Protein, CF

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. Dysregulation of suppressor of cytokine signaling 3 in keratinocytes causes skin inflammation mediated by interleukin-20 receptor-related cytokines.
    Authors: Uto-Konomi A, Miyauchi K, Ozaki N
    PLoS ONE, 2012;7(7):e40343.
    Species: Mouse
    Sample Types: Whole Tissue
    Applications: IHC-Fr
  2. Interleukin-23 and interleukin-27 exert quite different antitumor and vaccine effects on poorly immunogenic melanoma.
    Authors: Oniki S, Nagai H, Horikawa T, Furukawa J, Belladonna ML, Yoshimoto T, Hara I, Nishigori C
    Cancer Res., 2006;66(12):6395-404.
    Species: Mouse
    Sample Types: Cell Culture Supernates
    Applications: ELISA Developmet

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Reviews for Recombinant Mouse IL-23R Fc Chimera Protein, CF

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Recombinant Mouse IL-23 R Fc Chimera Protein, CF
By Anonymous on 01/08/2018
Application: Binding assay/Protein-protein interaction
Reason for Rating: Displayed binding characteristics in line with orthogonal experiments.

BLI experiment to assess the binding of IL-23 and mutants to IL-23R. Recombinant Mouse IL-23 R Fc Chimera Protein was immobilized on anti-human IgG Fc capture biosensors. Sensograms and fit of 1:1 model of 3 fold dilution series of analyte starting at 517 nM. (Bloch et al. Immunity 2018 DOI: http://dx.doi.org/10.1016/j.immuni.2017.12.008)