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Recombinant Rat ARRB2 Protein Pre-coupled Magnetic Beads

Cat.No. : ARRB2-459R-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.
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Source : HEK293
Species : Rat
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 Name : Arrb2 arrestin, beta 2 [ Rattus norvegicus ]
Official Symbol : ARRB2
Gene ID : 25388
mRNA Refseq : NM_012911.1
Protein Refseq : NP_037043.1
UniProt ID : P29067

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 (5)

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Can ARRB2 interact with other proteins? 10/10/2022

Yes, ARRB2 can interact with a variety of proteins to regulate GPCR signaling and participate in other cellular processes. It can interact with phosphorylated GPCRs to promote desensitization and internalization. ARRB2 also interacts with components of the endocytic machinery, such as clathrin and adaptor proteins, to facilitate receptor internalization. Additionally, ARRB2 can interact with downstream effectors, including kinases and scaffolding proteins, to mediate specific signaling events.

Can ARRB2 have non-canonical functions outside of GPCR signaling? 01/08/2020

Yes, studies have suggested that ARRB2 can have non-canonical functions independent of GPCR signaling. For instance, ARRB2 has been implicated in regulating cell migration, cell cycle progression, and apoptosis. It can also interact with and modulate the activity of various non-GPCR proteins, including ion channels, tyrosine kinase receptors, and cytoskeletal components. These non-canonical functions of ARRB2 expand its role beyond GPCR regulation.

What research is being conducted to explore the therapeutic potential of targeting ARRB2? 06/30/2017

Given its involvement in neurological and psychiatric disorders, there is ongoing research to explore the therapeutic potential of targeting ARRB2. Scientists are investigating the development of drugs that could modulate ARRB2 function, aiming to restore or enhance its normal signaling activity. Moreover, understanding the specific GPCRs and signaling pathways regulated by ARRB2 could help identify novel targets for therapeutic intervention in relevant diseases.

Are there any known genetic mutations or polymorphisms associated with ARRB2? 03/28/2016

Yes, genetic variations in the ARRB2 gene have been identified. Some single nucleotide polymorphisms (SNPs) in the ARRB2 gene have been associated with certain psychiatric disorders, like schizophrenia and bipolar disorder. These genetic variations may impact ARRB2 expression or function, potentially contributing to disease susceptibility or clinical phenotypes.

Are there any diseases associated with ARRB2 dysfunction? 02/14/2016

Dysregulation of ARRB2 has been linked to various neurological and psychiatric disorders. For example, alterations in ARRB2 expression and signaling have been observed in schizophrenia, bipolar disorder, and opioid addiction. These findings suggest that ARRB2 dysfunction may contribute to the pathogenesis of these conditions, making it a potential therapeutic target.

Customer Reviews (3)

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Reviews
09/07/2022

    the ARRB2 protein has proven to be an invaluable tool in protein electron microscopy structure analysis.

    06/30/2018

      Its exceptional reliability and compatibility with various research methodologies make it an invaluable asset for scientists seeking to delve into protein-protein interactions, signaling pathways, and structural investigations.

      12/12/2017

        Its robust nature and stability make it suitable for imaging studies, providing researchers with a detailed understanding of the protein's structural characteristics.

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