Recombinant Human IL10RB Protein (Leu87-Ala243), N-His tagged

• Cat.No.: IL10RB-1211H
• Product Overview: Recombinant Human CDw210b/IL10RB (Leu87-Ala243) fused with the N-His tag was expressed in E. coli.

Specification

• Source: E. coli
• Species: Human
• Tag: N-His
• Form: Lyophilized powder/frozen liquid
• Molecular Mass: 20.58 kDa
• Protein Length: Leu87-Ala243
• 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: 0.01M PBS, pH 7.4, 0.02% NLS
• Reconstitution: Reconstitute in sterile water for a stock solution.
• Shipping: They are shipped out with dry ice/blue ice unless customers require otherwise.

Gene Information

• Gene Name: IL10RB interleukin 10 receptor, beta [ Homo sapiens (human) ]
• Official Symbol: IL10RB
• Synonyms: IL10RB; interleukin 10 receptor, beta; CRFB4, D21S58, D21S66; interleukin-10 receptor subunit beta; CDW210B; CRF2 4; IL 10R2; IL-10RB; IL-10R subunit 2; IL-10R subunit beta; IL-10 receptor subunit beta; cytokine receptor class-II CRF2-4; interleukin-10 receptor subunit 2; cytokine receptor class-II member 4; cytokine receptor family 2 member 4; cytokine receptor family II, member 4; CRFB4; CRF2-4; D21S58; D21S66; IL-10R2
• Gene ID: 3588
• mRNA Refseq: NM_000628
• Protein Refseq: NP_000619
• MIM: 123889
• UniProt ID: Q08334

Reviews

04/28/2022

Reliable in co-immunoprecipitation.

06/13/2020

High specificity.

12/04/2019

Effective in signaling pathways.

Q&As

Can you explain the role of mass spectrometry-based interactomics in identifying IL10RB-interacting proteins?

Mass spectrometry-based interactomics identifies proteins interacting with IL10RB.

How does NMR spectroscopy help in understanding dynamic interactions and structural changes in IL10RB upon ligand binding?

NMR spectroscopy helps understand dynamic interactions and structural shifts in IL10RB upon binding.

How do proximity labeling and quantitative proteomics reveal changes in IL10RB's protein network upon IL-10 stimulation?

Proximity labeling and quantitative proteomics show IL10RB's changing protein network with IL-10.

How do techniques like surface plasmon resonance and isothermal titration calorimetry contribute to studying IL10RB-IL-10 binding kinetics?

Techniques like surface plasmon resonance and isothermal titration calorimetry measure IL10RB-IL-10 binding strength and kinetics.

What insights do flow cytometry and single-cell transcriptomics provide about IL10RB's expression across cell types and immune subsets?

Flow cytometry and single-cell transcriptomics reveal IL10RB's expression diversity in cells and immune subsets.

Could you explain how mutagenesis and alanine scanning identify critical amino acids in IL10RB's binding to IL-10?

Mutagenesis and alanine scanning pinpoint amino acids essential for IL10RB's binding to IL-10.

How are CRISPR-edited cell lines and gene knockout models utilized to explore IL10RB's downstream signaling pathways after IL-10 binding?

CRISPR-edited cells and knockout models explore IL10RB's signaling after IL-10 binding.

What methods are used to reveal structural changes in IL10RB upon interaction with IL-10, such as X-ray crystallography and cryo-electron microscopy?

X-ray crystallography and cryo-electron microscopy provide structural insights into IL10RB's changes upon IL-10 interaction.

What does genome-wide CRISPR screening reveal about genes and pathways influencing IL10RB expression and function?

Genome-wide CRISPR screening uncovers genes affecting IL10RB expression and function.

What experimental approaches, like co-immunoprecipitation and FRET, are used to study protein complexes involving IL10RB and IL-10?

Co-immunoprecipitation and FRET study protein complexes involving IL10RB and IL-10.