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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.>
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;

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) and IL-10R1 (Green) along with the binding interface (Red). Val33 indicates the location of a helical bend for the binding helix. (C) Mimicking of this interface could produce an antagonist to inhibit the interaction. The binding helical region of IL-10 (black) is aligned with designed peptides (P1 and P2 in Blue) along with the hydrophilic/hydrophobic (HP) pattern (Red). Two control peptides (P3 and P4) are also shown (Orange).

(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) and IL-10R1 (Green) along with the binding interface (Red). Val33 indicates the location of a helical bend for the binding helix. (C) Mimicking of this interface could produce an antagonist to inhibit the interaction. The binding helical region of IL-10 (black) is aligned with designed peptides (P1 and P2 in Blue) along with the hydrophilic/hydrophobic (HP) pattern (Red). Two control peptides (P3 and P4) are also shown (Orange).

(A) MALDI mass spectra of IL-10R1 when mixed with P1, P2 and P3 as shown. Only P1 and P2 displayed a peak corresponding to the mass of the complex structure. (B) An overlay of sensorgrams of the SPR competitive binding assay of peptides P1 and P2. Compared with sensorgrams with only IL-10 or the corresponding peptide at the same concentration, a loss in total response was observed when P1 or P2 were co-injected with IL-10. (C) IL-10R expression levels in 3×10 5 U937 with anti-human CD210 using flow cytometry: stimulated with different amount of LPS overnight; unstimulated and stimulated with LPS (4×10 ?3 μM), LPS (4×10 ?3 μM) + P1 (4.5 μM), P2 (4.1 μM), P3 (5.6 μM) or P4 (4.2 μM), and LPS (4×10 ?3 μM) + aIL10R1 overnight, respectively; the mean fluorescence intensity (MFI) result of IL10-R expression.

(A) MALDI mass spectra of IL-10R1 when mixed with P1, P2 and P3 as shown. Only P1 and P2 displayed a peak corresponding to the mass of the complex structure. (B) An overlay of sensorgrams of the SPR competitive binding assay of peptides P1 and P2. Compared with sensorgrams with only IL-10 or the corresponding peptide at the same concentration, a loss in total response was observed when P1 or P2 were co-injected with IL-10. (C) IL-10R expression levels in 3×10 5 U937 with anti-human CD210 using flow cytometry: stimulated with different amount of LPS overnight; unstimulated and stimulated with LPS (4×10 ?3 μM), LPS (4×10 ?3 μM) + P1 (4.5 μM), P2 (4.1 μM), P3 (5.6 μM) or P4 (4.2 μM), and LPS (4×10 ?3 μM) + aIL10R1 overnight, respectively; the mean fluorescence intensity (MFI) result of IL10-R expression.

Publication :
Investigation the Possibility of Using Peptides with a Helical Repeating Pattern of Hydro-Phobic and Hydrophilic Residues to Inhibit IL-10 (2016)
Developing a novel therapeutic vaccine combining IL-10 inhibitor for late stage cancers with targeted Clostridial spore oncolysis of the tumour microenvironment (2017)

Not For Human Consumption!

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Customer Reviews (3)

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Reviews
02/02/2021

    Good for receptor binding studies.

    11/19/2019

      Consistent in bioactivity.

      06/19/2017

        Suitable for ELISA.

        Q&As (10)

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        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? 09/23/2022

        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? 12/28/2021

        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? 05/03/2021

        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? 04/27/2021

        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? 07/24/2020

        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? 04/02/2020

        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? 03/07/2019

        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? 07/01/2018

        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? 07/19/2017

        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? 03/15/2017

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

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