Recombinant Human IL10RA Protein (Leu132-Asn235), His tagged

• Cat.No.: IL10RA-2993H
• Product Overview: Recombinant human IL10RA (Leu132-Asn235) protein fused with His tag was expressed in E. coli.

Specification

• Description: Cell surface receptor for the cytokine IL10 that participates in IL10-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. Once phosphorylated, STAT3 homodimerizes, translocates to the nucleus and activates the expression of anti-inflammatory genes. In addition, IL10RA-mediated activation of STAT3 inhibits starvation-induced autophagy.
• Source: E. coli
• Species: Human
• Tag: His
• Molecular Mass: 13.32 kDa
• Protein Length: Leu132-Asn235
• Purity: >90 % as determined by SDS-PAGE.
• Notes: For research use only.
• Storage: Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8 centigrade for one week. Store at -20 to -80 centigrade for twelve months from the date of receipt.
• Storage Buffer: Supplied as solution form in PBS pH 7.5 or lyophilized from PBS pH 7.5.
• Reconstitution: Reconstitute in sterile water for a stock solution.
• Shipping: In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.

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.