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IL-10 R alpha

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Cat. No. Species Product Description Structure Purity Feature
ILR-H82F6 Human Biotinylated Human IL-10 R alpha / CD210 Protein, Fc,Avitag™ (MALS verified)
ILR-H82F6-structure
ILR-H82F6-sds

Part of Bioactivity data

ILR-H82F6-MALS-HPLC
Biotinylated Human IL-10 R alpha, Fc,Avitag (Cat. No. ) MALS images

The purity of Biotinylated Human IL-10 R alpha, Fc,Avitag (Cat. No. ILR-H82F6) is more than 90% and the molecular weight of this protein is around 124-152 kDa verified by SEC-MALS.

Bioactivity-ELISA
Biotinylated Human IL-10 R alpha, Fc,AvitagBiotinylated Human IL-10 R alpha, Fc,Avitag (Cat. No. ILR-H82F6) ELISA bioactivity

Immobilized Human IL-10, His Tag (Cat. No. IL0-H4248) at 5 μg/mL (100 μL/well) can bind Biotinylated Human IL-10 R alpha, Fc,Avitag (Cat. No. ILR-H82F6) with a linear range of 0.2-10 ng/mL (QC tested).

ILR-H82F6-ELISA
Biotinylated Human IL-10 R alpha, Fc,AvitagBiotinylated Human IL-10 R alpha, Fc,Avitag (Cat. No. ILR-H82F6) ELISA bioactivity

Immobilized Human IL-10, His Tag (Cat. No. IL0-H4248) at 5 μg/mL (100 μL/well) can bind Biotinylated Human IL-10 R alpha, Fc,Avitag (Cat. No. ILR-H82F6) with a linear range of 0.2-10 ng/mL (QC tested).

Synonym Name

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,CD210,IL10RA,IL10R

Background

Interleukin-10 receptor subunit alpha (IL-10 R alpha ) is a cell surface receptor for the cytokine IL-10 that participates in IL-10 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.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.These kinases then phosphorylate specific tyrosine residues in the intracellular domain in IL10RA leading to the recruitment and subsequent phosphorylation of STAT3.

Clinical and Translational Updates

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