Recombinant Human IL10RA Protein, His-tagged

• Cat.No.: IL10RA-073H
• Product Overview: Recombinant Human IL10RA Protein with His tag was expressed in E. coli.

Specification

• Description: The IL-10 receptor, IL-10R, is a member of the class II subgroup of the cytokine receptor family and exhibits structural similarity to the interferon receptor. IL-10R is expressed in B cells and T helper cells, as well as in LPS-induced mouse fibroblasts. Overall, mouse IL-10R and human IL-10R share 60% sequence identity at the protein level. Stimulation with IL-10 leads to phosphorylation of JAK1 and Tyk 2 tyrosine kinases. The activated kinases phosphorylate the two tyrosine residues (Tyr 446 and Tyr 496) in the cytoplasmic domain of IL-10Rα. The phosphorylation of these two residues are required for proper function of IL-10R and activation of IL-10E1 signaling. IL-10Rβ is ubiquitously expressed and, in addition to forming the IL-10 heterodimeric receptor, it forms a heterodimeric receptor with an IL-22R subunit and an IL-28R subunit. IL-10R is constitutively expressed on human natural killer (NK) cells and the direct binding of IL-10 potentiates cytokine production by human NK cells.
• Source: E. coli
• Species: Human
• Tag: His
• Molecular Mass: ~26 kDa
• AA Sequence: HGTELPSPPSVWFEAEFFHHILHWT PIPNQSESTCYEVALLRYGIESWNS ISNCSQTLSYDLTAVTLDLYHSNGY RARVRAVDGSRHSNWTVTNTRFSVD EVTLTVGSVNLEIHNGFILGKIQLP RPKMAPANDTYESIFSHFREYEIAI RKVPGNFTFTHKKVKHENFSLLTSG EVGEFCVQVKPSVASRSNKGMWSKE ECISLTRQYFTVTN
• Purity: Transferred into competent cells and the supernatant was purified by NI column affinity chromatography and the purity is > 85% (by SDS-PAGE).
• Notes: For research use only, not for use in diagnostic procedure.
• Storage: Store at 4 centigrade short term. Aliquot and store at -20 centigrade long term. Avoid freeze-thaw cycles.
• Storage Buffer: PBS, 4M Urea, pH7.4

Gene Information

• Gene Name: IL10RA interleukin 10 receptor, alpha [ Homo sapiens (human) ]
• 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

Reviews

02/02/2021

Good for receptor binding studies.

11/19/2019

Consistent in bioactivity.

06/19/2017

Suitable for ELISA.

Q&As

How are innovative experimental techniques like surface plasmon resonance and isothermal titration calorimetry utilized to study the binding kinetics between IL-10RA and its ligand IL-10?

Surface plasmon resonance and isothermal titration calorimetry techniques quantify binding kinetics between IL10RA and IL-10, revealing affinity and association/dissociation rates.

How are cutting-edge flow cytometry and single-cell transcriptomics techniques applied to dissect the heterogeneity in IL10RA expression across different immune cell subsets?

Cutting-edge flow cytometry and single-cell transcriptomics uncover the expression patterns of IL10RA across diverse immune cell subsets.

How do researchers employ biophysical techniques like nuclear magnetic resonance (NMR) spectroscopy to unravel the dynamic interactions between IL10RA and IL-10 at the molecular level?

NMR spectroscopy captures dynamic interactions, revealing the flexibility and movements of IL10RA and IL-10 during their binding events.

Could you provide insights into the comprehensive experimental methodologies, such as surface proteomics and mass spectrometry, used to identify potential IL10RA-interacting partners in complex cellular environments?

Surface proteomics and mass spectrometry identify proteins physically interacting with IL10RA, providing insights into its complex functional networks.

What innovative approaches, such as proximity labeling and quantitative proteomics, are employed to uncover dynamic changes in IL10RA-associated protein networks upon IL-10 stimulation?

Proximity labeling and quantitative proteomics unveil dynamic changes in IL10RA-associated proteins, shedding light on response mechanisms.

Could you explain the complex experimental methodologies employed to investigate the conformational changes in IL10RA upon ligand binding using techniques like X-ray crystallography and cryo-electron microscopy?

X-ray crystallography and cryo-electron microscopy provide detailed structural insights into the changes in IL10RA's 3D arrangement upon binding to IL-10.

What advanced strategies, such as site-directed mutagenesis and alanine scanning, are used to pinpoint the critical amino acid residues in IL10RA that are essential for its interaction with IL-10?

Site-directed mutagenesis and alanine scanning pinpoint key amino acids in IL10RA essential for IL-10 interaction, aiding in understanding binding determinants.

How do researchers leverage advanced genome-wide CRISPR screening techniques to systematically identify genes and pathways that modulate IL10RA expression and function in various physiological contexts?

Genome-wide CRISPR screening identifies genes and pathways affecting IL10RA expression and function, aiding in understanding its regulatory network.

Can you elaborate on the sophisticated experimental approaches, such as co-immunoprecipitation and F枚rster resonance energy transfer (FRET), used to explore the formation of IL10RA-IL-10 receptor complexes?

Co-immunoprecipitation and FRET techniques elucidate the assembly of multi-protein IL10RA-IL-10 receptor complexes in cellular environments.

What state-of-the-art experimental designs, including CRISPR/Cas9-edited cell lines and gene knockout models, are harnessed to study the downstream signaling cascades initiated by IL10RA activation?

CRISPR/Cas9-modified cell lines and gene knockout models help dissect intricate signaling pathways activated by IL10RA upon ligand engagement.