Recombinant Human IL-23R Fc Chimera Avi-tag Protein, CF
Recombinant Human IL-23R Fc Chimera Avi-tag Protein, CF Summary
Learn more about Avi-tag Biotinylated ProteinsProduct Specifications
Human IL-23R (Gly24-Asp353) Accession # AAM44229.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag |
N-terminus | C-terminus | ||
Analysis
Product Datasheets
Carrier Free
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.
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.
AVI1400
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 250 μg/mL in 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.
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Scientific Data
When Recombinant Human IL-23 Protein (1290-IL) is immobilized at 1.0 µg/mL (100 µL/well), the concentration of Biotinylated Recombinant Human IL-23R Fc Chimera Avi-tag Protein (Catalog # AVI1400) that produces 50% of the optimal binding response is 10.0-100 ng/mL.
2 μg/lane of Biotinylated Recombinant Human IL-23R Fc Chimera Avi-tag Protein (Catalog # AVI1400) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 90-102 kDa and 180-200 kDa, respectively.
Reconstitution Calculator
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). 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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