Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Additional Information | Biotinylated |
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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. |
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Source | Human embryonic kidney cell, HEK293-derived human IL-23R protein
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N-terminal Sequence | Gly24 |
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Structure / Form | Disulfide-linked homodimer Biotinylated via Avi-tag |
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Protein/Peptide Type | Recombinant Proteins |
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Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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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. |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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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. |
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.
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