Recombinant Human IL-23R Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit IL-23 induced IL-17 secretion by mouse splenocytes. The ED 50 for this effect is 0.008-0.04 µg/mL in the presence of 0.3 ng/mL of rhIL-23.
Source
Mouse myeloma cell line, NS0-derived human IL-23 R protein
>95%, 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
64 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
95-105 kDa, reducing conditions
Publications
Read Publications using 1400-IR in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, 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-23R Fc Chimera Protein, CF
IBD17
IL-23 R
IL-23 receptor
IL23R
IL-23R
interleukin 23 receptor
interleukin-23 receptor
Background
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). Human IL-23 R cDNA encodes a 629 aa type I transmembrane protein with a 23 aa residue signal peptide, a 330 aa residue extracellular domain, a 23 aa residue transmembrane domain and a 253 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. Based on quantitative real-time PCR, human IL-23 R mRNA is expressed in a human Th1 and Th0 clone as well as several NK cell lines and clones. Low but detectable levels of IL-23 R mRNA is also expressed in EBV-transformed B cells and activated PBMC. 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.
Oppmann, B. et al. (2000) Immunity 13:715.
Lankford, C.S. and D.M. Frucht (2003) J. Leukoc. Biol. 73:49.
Parham, C. et al. (2002) J. Immunol. 168:5448.
Belladonna, M.L. et al. (2002) J. Immunol. 168:5448.
Aggarwal, S. et al. (2003) J. Biol. Chem. 278:1910.
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