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Active Recombinant human IL10RA Protein, Fc-tagged

Cat.No. : IL10RA-02H
Product Overview : Recombinant Human IL10RA Protein(Q13651)(His 22 - Asn 235), fused with Fc tag, was expressed in HEK293.
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  • Gene Information
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Source : HEK293
Species : Human
Tag : Fc
Form : Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.
Bio-activity : Immobilized Human IL-10, His Tag at 5 μg/mL (100 μL/well) can bind Human IL-10 R alpha / CD210, Fc Tag with a linear range of 0.2-2 ng/mL.
Molecular Mass : The protein has a calculated MW of 50.8 kDa. The protein migrates as 65-75 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Protein Length : His 22 - Asn 235
Endotoxin : Less than 1.0 EU per μg by the LAL method.
Purity : >95% as determined by SDS-PAGE.
Storage : For long term storage, the product should be stored at lyophilized state at -20 centigrade or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
-20 centigrade to -70 centigrade for 12 months in lyophilized state;
-70 centigrade for 3 months under sterile conditions after reconstitution.
Reconstitution : It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4℃ before opening to recover the entire contents.
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

For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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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.

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.

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