Recombinant Cynomolgus Monkey IL-23R Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human IL-23 Protein
(Catalog #
1290-IL)
is immobilized at 1 μg/mL (100 μL/well), the concentration of Recombinant Cynomolgus Monkey IL-23R Fc Chimera (Catalog # 10306-IR) that produces 50% of the optimal binding response is found to be approximately 50-250 ng/mL. |
Source |
Human embryonic kidney cell, HEK293-derived cynomolgus monkey IL-23R protein Cynomolgus Monkey IL-23R (Gly24-Asp353) Accession # XP_005543141 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Gly24 |
Structure / Form |
Disulfide-linked homodimer |
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 |
|
Theoretical MW |
65 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 |
91-102 kDa, under reducing conditions |
Packaging, Storage & Formulations
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.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 200 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Cynomolgus Monkey IL-23R Fc Chimera Protein, CF
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 amino acid (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 (6). 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. Based on quantitative real-time PCR, human
IL-23 R mRNA is expressed in a human TH0, TH1 as well as several NK
cell lines. 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 (2). The Cynomolgus IL-23 R shares 96%, 71% and 77% amino
acid sequence identity to Human, mouse, and rat IL-23 R, respectively.
- Oppmann, B. et al. (2000) Immunity 13:715.
- Lankford, C.S. and Frucht, D.M. (2003) J. Leukoc. Biol. 73:49.
- Parham, C. et al. (2002) J. Immunol. 168:5699.
- Belladonna, M.L. et al. (2002) J. Immunol. 168:5448.
- Aggarwal, S. et al. (2003) J. Biol. Chem. 278:1910.
- Schroder, J. et al. (2015) J. Biol. Chem. 290:359.
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