Recombinant Human IL-23R Fc Chimera Avi-tag Protein, CF Summary
| Additional Information |
Biotinylated |
| Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human IL-23 Protein (Catalog # 1290-IL) is immobilized at 1.0 µg/mL (100 µL/well), the concentration of Biotinylated Recombinant Human IL-23R Fc Chimera Avi-tag (Catalog # AVI1400) that produces 50% of the optimal binding response is 10.0-100 ng/mL. |
| Source |
Human embryonic kidney cell, HEK293-derived human IL-23R protein | Human IL-23R (Gly24-Asp353) Accession # AAM44229.1 | IEGRMD | Human IgG 1 (Pro100-Lys330) | Avi-tag | N-terminus | | | C-terminus | |
| N-terminal Sequence |
Gly24 |
| Structure / Form |
Disulfide-linked homodimer Biotinylated via Avi-tag |
| 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 |
66 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 |
90-102 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 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 with Trehalose. |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Reconstitution Instructions |
Reconstitute at 250 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 Human IL-23R Fc Chimera Avi-tag 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 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. Our Avi-tag Biotinylated human IL-23R Fc chimera features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
- 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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