Recombinant Mouse Il10ra protein, His & GST-tagged

• Cat.No.: Il10ra-1726M
• Product Overview: Recombinant Mouse Il10ra aa. (Leu17~Ile241) fused with N-terminal His & GST tag was produced in E. coli cells.

Specification

• Source: E. coli
• Species: Mouse
• Tag: His & GST
• Form: Freeze-dried powder
• Molecular Mass: 57kDa as determined by SDS-PAGE reducing conditions.
• Protein length: Leu17~Ile241
• Endotoxin: <1.0EU per 1ug (determined by the LAL method)
• Purity: >98%
• Characteristic: The isoelectric point is 6.8.
• Applications: Positive Control; Immunogen; SDS-PAGE; WB.
• Stability: The thermal stability is described by the loss rate of the target protein. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37°C for 48h, and no obvious degradation and precipitation were observed. (Referring from China Biological Products Standard, which was calculated by the Arrhenius equation.) The loss of this protein is less than 5% within the expiration date under appropriate storage condition.
• Storage: Avoid repeated freeze/thaw cycles. Store at 2-8°C for one month. Aliquot and store at -80°C for 12 months.
• Concentration: 200ug/mL
• Storage buffer: 100mM NaHCO3, 500mM NaCl, pH8.3, containing 1mM EDTA, 1mM DTT, 0.01% sarcosyl, 5%Trehalose and Proclin300.
• Reconstitution: Reconstitute in 100mM NaHCO3, 500mM NaCl (pH8.3) to a concentration of 0.1-1.0 mg/mL. Do not vortex.

Gene Information

• Gene Name: Il10ra interleukin 10 receptor, alpha [ Mus musculus (house mouse) ]
• Official Symbol: Il10ra
• Synonyms: Il10ra; interleukin 10 receptor, alpha; Il10r; CDw210; CDw210a; IL-10R1; IL-10RA; mIL-10R; AW553859; interleukin-10 receptor subunit alpha; IL-10 receptor subunit alpha; IL-10R subunit 1; IL-10R subunit alpha; interleukin-10 receptor subunit 1
• Gene ID: 16154
• mRNA Refseq: NM_008348.3
• Protein Refseq: NP_032374.1
• UniProt ID: Q61727

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.