Recombinant Human IL10RB Protein Pre-coupled Magnetic Beads

• Cat.No.: IL10RB-4431H-B
• Product Overview: The Recombnant protein was conjugated to magnetic beads. This ready-to-use, pre-coupled magnetic beads are in uniform particle size and narrow size distribution with large surface area, which is conducive to convenient and fast capture target molecules with high specificity and achieve magnetic separation. This product can be equipped with automation equipment for high-throughput operations.

Specification

• Source: HEK293
• Species: Human
• Form: Solution
• Particle size: ~2 μm
• Beads Surface: Hydrophilic
• Capacity: > 200 pmol rabbit IgG/ mg beads
• Applications: Immunoassay, In vitro diagnostics, cell sorting, Immunoprecipitation/Co-precipitation, Protein/antibody separation and purification.
• Stability: Stable for at least 6 months from the date of receipt of the product under proper storage and handling conditions.
• Storage: 2-8℃. Do not to freeze thaw the Beads
• Concentration: 10mg beads/mL
• Storage Buffer: PBS buffer

Gene Information

• Gene Name: IL10RB interleukin 10 receptor, beta [ Homo sapiens ]
• Synonyms: IL10RB; erleukin 10 receptor, beta; CRFB4; CRF2-4; D21S58; D21S66; CDW210B; IL-10R2; cytokine receptor class-II CRF2-4; cytokine receptor family II, member 4; IL-10R-B; Interleukin-10 receptor beta chain
• 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.