Recombinant Human ARRB2 Protein, Tag Free
Cat.No. : | ARRB2-0341H |
Product Overview : | Recombinant human ARRB2 Protein without tag was expressed in E.coli. |
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Source : | E. coli |
Species : | Human |
Tag : | Tag Free |
Form : | Lyophilized powder/frozen liquid |
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 : | They are shipped out with dry ice/blue ice unless customers require otherwise. |
Gene Name : | ARRB2 arrestin, beta 2 [ Homo sapiens (human) ] |
Official Symbol : | ARRB2 |
Synonyms : | ARRB2; arrestin, beta 2; ARR2; beta-arrestin-2; arrestin 3; BARR2; DKFZp686L0365; arrestin beta-2; ARB2; |
Gene ID : | 409 |
mRNA Refseq : | NM_001257328 |
Protein Refseq : | NP_001244257 |
MIM : | 107941 |
UniProt ID : | P32121 |
Products Types
◆ Recombinant Protein | ||
ARRB2-459R | Recombinant Rat ARRB2 Protein, His (Fc)-Avi-tagged | +Inquiry |
ARRb2-3639H | Recombinant Human ARRb2 protein(Asp262~Cys430), His-GST-tagged | +Inquiry |
ARRB2-803R | Recombinant Rat ARRB2 Protein | +Inquiry |
ARRB2-0340H | Recombinant Human ARRB2 Protein (Met1-Cys409), C-His-tagged | +Inquiry |
ARRB2-855H | Recombinant Human ARRB2 protein, GST-tagged | +Inquiry |
◆ Lysates | ||
ARRB2-130HCL | Recombinant Human ARRB2 cell lysate | +Inquiry |
Related Gene
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)
Ask a questionYes, 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.
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.
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.
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.
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)
Write a reviewthe ARRB2 protein has proven to be an invaluable tool in protein electron microscopy structure analysis.
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.
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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