Active Recombinant Human IL10RA, HIgG1 Fc-tagged
Cat.No. : | IL10RA-212H |
Product Overview : | The extracellular domain of human IL-10RA (AAH28082.1) (His22-Asn235) is fused to the N-terminus of the Fc region of a human IgG1 was expressed in CHO cell. |
Availability | February 15, 2025 |
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Description : | The protein encoded by this gene is a receptor for interleukin 10. This protein is structurally related to interferon receptors. It has been shown to mediate the immunosuppressive signal of interleukin 10, and thus inhibits the synthesis of proinflammatory cytokines. This receptor is reported to promote survival of progenitor myeloid cells through the insulin receptor substrate-2/PI 3-kinase/AKT pathway. Activation of this receptor leads to tyrosine phosphorylation of JAK1 and TYK2 kinases. Two transcript variants, one protein-coding and the other not protein-coding, have been found for this gene. |
Source : | CHO cell |
Species : | Human |
Tag : | HIgG1 Fc-tagged |
Form : | Lyophilized from 0.2μm-filtered solution in PBS. |
Bio-activity : | Measured by its ability to inhibit IL-10-dependent proliferation of MC/92 mouse mast cells. |
Molecular Mass : | 51KDa (monomer) |
AA Sequence : | His22-Asn235 |
Endotoxin : | <0.06 eu/μg as determined by lal test.>0.06> |
Purity : | >98%, by SDS-PAGE under reducing conditions. |
Stability : | Stable for at least 1 year after receipt when stored at -20°C. Working aliquots are stable for up to 3 months when stored at -20°C. |
Reconstitution : | Reconstitute at 100μg/ml in sterile PBS. |
Warning : | Avoid freeze/thaw cycles. |
Protein length : | His22-Asn235 |
Gene Name : | IL10RA interleukin 10 receptor, alpha [ Homo sapiens ] |
Official Symbol : | IL10RA |
Synonyms : | IL10RA; interleukin 10 receptor, alpha; IL10R; interleukin-10 receptor subunit alpha; CD210; CD210a; CDW210A; HIL 10R; IL-10RA; IL-10R subunit 1; IL-10R subunit alpha; IL-10 receptor subunit alpha; interleukin-10 receptor subunit 1; interleukin-10 receptor alpha chain; HIL-10R; IL-10R1; |
Gene ID : | 3587 |
mRNA Refseq : | NM_001558 |
Protein Refseq : | NP_001549 |
MIM : | 146933 |
UniProt ID : | Q13651 |
Chromosome Location : | 11q23 |
Pathway : | Cytokine-cytokine receptor interaction, organism-specific biosystem; Cytokine-cytokine receptor interaction, conserved biosystem; Jak-STAT signaling pathway, organism-specific biosystem; Jak-STAT signaling pathway, conserved biosystem; Toxoplasmosis, organism-specific biosystem; Toxoplasmosis, conserved biosystem; Tuberculosis, organism-specific biosystem; |
Function : | interleukin-10 receptor activity; protein binding; receptor activity; signal transducer activity; |
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Related Gene
Investigation the Possibility of Using Peptides with a Helical Repeating Pattern of Hydro-Phobic and Hydrophilic Residues to Inhibit IL-10
Journal: PLoS ONE PubMed ID: 27100390 Data: 2016/4/21
Authors: Guoying Ni, Shu Chen, Massimiliano Galdiero
Article Snippet:Lipopolysaccharide (LPS) and Incomplete Freund’s adjuvant (IFA) were purchased from Sigma.Lipopolysaccharide (LPS) and Incomplete Freund’s adjuvant (IFA) were purchased from Sigma.. Recombinant Human interleukin 10 receptor alpha was purchased from Creative BioMart, USA (Cat. No IL10RA-212H), and was re-suspended in sterilized Milli Q water to a concentration of 1 μg/μL as stock solution.. Recombinant Human interleukin 5 receptor alpha was purchased from Genscript, USA (Cat. No Z03126-10), and was re-suspended in sterilized Milli Q water to a concentration of 1 μg/μL as stock solution.Recombinant Human interleukin 5 receptor alpha was purchased from Genscript, USA (Cat. No Z03126-10), and was re-suspended in sterilized Milli Q water to a concentration of 1 μg/μL as stock solution.

(A) A space-filling model of the interface structure of the IL-10/IL-10R protein–protein complex. (B) An expansion of the interface between the two proteins to indicate a few residue to residue contacts. The complex structure of IL-10 (Grey)

(A) MALDI mass spectra
Not For Human Consumption!
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Customer Reviews (3)
Write a reviewGood for receptor binding studies.
Consistent in bioactivity.
Suitable for ELISA.
Q&As (10)
Ask a questionSurface plasmon resonance and isothermal titration calorimetry techniques quantify binding kinetics between IL10RA and IL-10, revealing affinity and association/dissociation rates.
Cutting-edge flow cytometry and single-cell transcriptomics uncover the expression patterns of IL10RA across diverse immune cell subsets.
NMR spectroscopy captures dynamic interactions, revealing the flexibility and movements of IL10RA and IL-10 during their binding events.
Surface proteomics and mass spectrometry identify proteins physically interacting with IL10RA, providing insights into its complex functional networks.
Proximity labeling and quantitative proteomics unveil dynamic changes in IL10RA-associated proteins, shedding light on response mechanisms.
X-ray crystallography and cryo-electron microscopy provide detailed structural insights into the changes in IL10RA's 3D arrangement upon binding to IL-10.
Site-directed mutagenesis and alanine scanning pinpoint key amino acids in IL10RA essential for IL-10 interaction, aiding in understanding binding determinants.
Genome-wide CRISPR screening identifies genes and pathways affecting IL10RA expression and function, aiding in understanding its regulatory network.
Co-immunoprecipitation and FRET techniques elucidate the assembly of multi-protein IL10RA-IL-10 receptor complexes in cellular environments.
CRISPR/Cas9-modified cell lines and gene knockout models help dissect intricate signaling pathways activated by IL10RA upon ligand engagement.
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