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 | The interleukin-10 receptor alpha (IL10RA) gene codes for the alpha chain of the IL-10 receptor which binds the cytokine IL-10. IL-10 is an anti-inflammatory cytokine with immunoregulatory function during the pathogenesis of many inflammatory disorders in livestock, including Johne's disease (JD). JD is a chronic enteritis in cattle caused by Mycobacterium avium subsp. paratuberculosis (MAP) and is responsible for significant economic losses to the dairy industry. Several candidate genes including IL10RA have been found to be associated with JD. |
molecular weight | The protein has a predicted MW of 27 kDa. Due to glycosylation, the protein migrates to 42-60 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Biotinylated Human IL-10 R alpha Protein 5031
$525.00 – $1,750.00
Summary
- Expression: HEK293
- Functional: Yes (ELISA)
- Amino Acid Range: His22-Asn235
Biotinylated Human IL-10 R alpha Protein 5031
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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The interleukin-10 receptor alpha (IL10RA) gene codes for the alpha chain of the IL-10 receptor which binds the cytokine IL-10. IL-10 is an anti-inflammatory cytokine with immunoregulatory function during the pathogenesis of many inflammatory disorders in livestock, including Johne's disease (JD). JD is a chronic enteritis in cattle caused by Mycobacterium avium subsp. paratuberculosis (MAP) and is responsible for significant economic losses to the dairy industry. Several candidate genes including IL10RA have been found to be associated with JD. |
Protein names Interleukin-10 receptor subunit alpha (IL-10 receptor subunit alpha) (IL-10R subunit alpha) (IL-10RA) (CDw210a) (Interleukin-10 receptor subunit 1) (IL-10R subunit 1) (IL-10R1) (CD antigen CD210) |
Gene names IL10RA,IL10RA IL10R |
Protein family Type II cytokine receptor family |
Mass 9606Da |
Function Cell surface receptor for the cytokine IL10 that participates in IL10-mediated anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Upon binding to IL10, induces a conformational change in IL10RB, allowing IL10RB to bind IL10 as well (PubMed:16982608). In turn, the heterotetrameric assembly complex, composed of two subunits of IL10RA and IL10RB, activates the kinases JAK1 and TYK2 that are constitutively associated with IL10RA and IL10RB respectively (PubMed:12133952). These kinases then phosphorylate specific tyrosine residues in the intracellular domain in IL10RA leading to the recruitment and subsequent phosphorylation of STAT3. Once phosphorylated, STAT3 homodimerizes, translocates to the nucleus and activates the expression of anti-inflammatory genes. In addition, IL10RA-mediated activation of STAT3 inhibits starvation-induced autophagy (PubMed:26962683). |
Subellular location Cell membrane ; Single-pass type I membrane protein. Cytoplasm . |
Tissues Primarily expressed in hematopoetic cells including B-cells, T-cells, NK cells, monocytes and macrophages. Not expressed in non-hematopoetic cells such as fibroblasts or endothelial cells. |
Structure Interacts with IL10 (PubMed:15837194, PubMed:16982608). Interacts with IL10RB (PubMed:16982608). Interacts (via its cytoplasmic domain) with JAK1 (via N-terminus) (PubMed:12133952). Interacts with BTRC; this interaction leads to IL10RA ubiquitination and subsequent degradation (PubMed:22087322). Interacts with STAT3 (By similarity).; (Microbial infection) Interacts with human cytomegalovirus protein IL10.; (Microbial infection) Interacts with Epstein-Barr virus protein IL10. |
Post-translational modification Phosphorylated. Phosphorylation of the cytoplasmic tail induced STAT3 activation.; Ubiquitinated by BTRC; ubiquitination leads to endocytosis and subsequent degradation of IL10RA. |
Target Relevance information above includes information from UniProt accession: Q13651 |
The UniProt Consortium |
Publications
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