Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
express system | HEK293 |
product tag | C-His-Avi |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
background | Although interferon (IFN)-α is known to exert immunomodulatory and antiproliferative effects on dendritic cells (DCs) through induction of protein-coding IFN-stimulated genes (ISGs), little is known about IFN-α-regulated miRNAs in DCs. Since several miRNAs are involved in regulating DC functions, it is important to investigate whether IFN-α's effects on DCs are mediated through miRNAs as well. |
molecular weight | The protein has a predicted MW of 28.34 kDa. Due to glycosylation, the protein migrates to 50-70 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Biotinylated Mouse IFN alpha/beta R2 Protein 2052
$525.00 – $1,750.00
Summary
- Expression: HEK293
- Binding assay: Yes (SPR)
- Amino Acid Range: Ser22-Ala242
Biotinylated Mouse IFN alpha/beta R2 Protein 2052
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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Although interferon (IFN)-α is known to exert immunomodulatory and antiproliferative effects on dendritic cells (DCs) through induction of protein-coding IFN-stimulated genes (ISGs), little is known about IFN-α-regulated miRNAs in DCs. Since several miRNAs are involved in regulating DC functions, it is important to investigate whether IFN-α's effects on DCs are mediated through miRNAs as well. |
Protein names Interferon alpha/beta receptor 2 (IFN-R-2) (IFN-alpha/beta receptor 2) (Type I interferon receptor 2) |
Gene names Ifnar2,Ifnar2 |
Protein family Type II cytokine receptor family |
Mass 10090Da |
Function Together with IFNAR1, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa). Type I interferon binding activates the JAK-STAT signaling cascade, resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response. Mechanistically, type I interferon-binding brings the IFNAR1 and IFNAR2 subunits into close proximity with one another, driving their associated Janus kinases (JAKs) (TYK2 bound to IFNAR1 and JAK1 bound to IFNAR2) to cross-phosphorylate one another. The activated kinases phosphorylate specific tyrosine residues on the intracellular domains of IFNAR1 and IFNAR2, forming docking sites for the STAT transcription factors (STAT1, STAT2 and STAT). STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes.; [Isoform 2]: May be potent inhibitors of type I IFN receptor activity.; [Isoform 3]: May be potent inhibitors of type I IFN receptor activity. |
Subellular location [Isoform 1]: Cell membrane ; Single-pass type I membrane protein .; [Isoform 2]: Secreted .; [Isoform 3]: Secreted . |
Tissues Widely expressed. Detected in liver, testis, kidney, salivary gland, thymus, brain, lung and placenta. Isoform 1, isoform 2 and isoform 3 are expressed in brain. |
Structure Heterodimer with IFNAR1; forming the receptor for type I interferon. Interacts with the transcriptional factors STAT1 and STAT2. Interacts with JAK1. Interacts with USP18; indirectly via STAT2, it negatively regulates the assembly of the ternary interferon-IFNAR1-IFNAR2 complex and therefore type I interferon signaling. |
Post-translational modification Phosphorylated on tyrosine residues upon interferon binding. Phosphorylation at Tyr-335 or Tyr-510 are sufficient to mediate interferon dependent activation of STAT1, STAT2 and STAT3 leading to antiproliferative effects on many different cell types (By similarity). |
Target Relevance information above includes information from UniProt accession: O35664 |
The UniProt Consortium |
Publications
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