Recombinant Mouse Beta-arrestin-1 (Arrb1)

Code CSB-YP805351MO
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Source Yeast
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Code CSB-EP805351MO
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Source E.coli
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Code CSB-EP805351MO-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP805351MO
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Source Baculovirus
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Code CSB-MP805351MO
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Source Mammalian cell
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Product Details

>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
Arrb1Beta-arrestin-1; Arrestin beta-1
Mus musculus (Mouse)
Expression Region
Target Protein Sequence
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Please contact us to get it.

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Target Background

Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Involved in internalization of P2RY4 and UTP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 ands subsequent recycling. Involved in the degradation of cAMP by recruiting cAMP phosphodiesterases to ligand-activated receptors. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2). ERK1/2 activated by the beta-arrestin scaffold is largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Recruits c-Src/SRC to ADRB2 resulting in ERK activation. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Inhibits ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Is required for SP-stimulated endocytosis of NK1R and recruits c-Src/SRC to internalized NK1R resulting in ERK1/2 activation, which is required for the antiapoptotic effects of SP. Is involved in proteinase-activated F2RL1-mediated ERK activity. Acts as signaling scaffold for the AKT1 pathway. Is involved in alpha-thrombin-stimulated AKT1 signaling. Is involved in IGF1-stimulated AKT1 signaling leading to increased protection from apoptosis. Involved in activation of the p38 MAPK signaling pathway and in actin bundle formation. Involved in F2RL1-mediated cytoskeletal rearrangement and chemotaxis. Involved in AGTR1-mediated stress fiber formation by acting together with GNAQ to activate RHOA. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. May serve as nuclear messenger for GPCRs. Involved in OPRD1-stimulated transcriptional regulation by translocating to CDKN1B and FOS promoter regions and recruiting EP300 resulting in acetylation of histone H4. Involved in regulation of LEF1 transcriptional activity via interaction with DVL1 and/or DVL2 Also involved in regulation of receptors other than GPCRs. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Involved in IL8-mediated granule release in neutrophils. Binds phosphoinositides. Binds inositolhexakisphosphate (InsP6). Required for atypical chemokine receptor ACKR2-induced RAC1-LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Involved in the internalization of the atypical chemokine receptor ACKR3. Negatively regulates the NOTCH signaling pathway by mediating the ubiquitination and degradation of NOTCH1 by ITCH. Participates in the recruitment of the ubiquitin-protein ligase to the receptor.
Gene References into Functions
  1. GPCR-arrestin complex initiates non-desensitized signalling at the plasma membrane by coupling with ion channels. PMID: 28181498
  2. beta-arrestin-1 promotes PPARalpha- but represses PPARgamma-mediated transcriptional activities, providing potential regulatory pathway for brown adipose tissue function. PMID: 27301785
  3. Our data reveal beta-arrestin 1, beta-arrestin 2, and AT1R as key regulatory molecules in the Frank-Starling mechanism, which involves length-dependent enhancement of cardiac myofilament Ca(2+) sensitivity. PMID: 27911784
  4. Arrb1 reduced the chemotherapy-induced Lgr5 stem cell apoptosis by inhibiting endoplasmic reticulum stress-mediated mitochondrial apoptotic signaling. PMID: 27195676
  5. findings suggest that knockdown of beta-arrestin 1 can suppress glioblastoma multiforme cell proliferation, invasion and glycolysis by inhibiting Src signaling PMID: 28442265
  6. Results revealed that beta-arrestin-1 regulates lactate metabolism to contribute to beta2-adrenergic receptor functions in improved memory formation. PMID: 27916196
  7. Study reports an X-ray free electron laser crystal structure of the rhodopsin-arrestin complex, in which the phosphorylated C terminus of rhodopsin forms an extended intermolecular beta sheet with the N-terminal beta strands of arrestin. Phosphorylation was detected at rhodopsin C-terminal tail residues T336 and S338. PMID: 28753425
  8. Beta-arrestin-1 with beta-arrestin-2 shared common mechanisms to suppress podocyte autophagy by negative regulation of ATG12-ATG5 conjugation. PMID: 27054338
  9. data suggest that beta-arr1 mediated nuclear signaling regulates the production of excretive factors derived from niche astrocytes and expansion of neural precursors in DG, thus maintaining homeostasis of adult hippocampal neurogenesis PMID: 26500013
  10. beta-arr1 has a critical role in modulating ERK, JNK and p38 MAPK pathways mediated by TNF-alpha in intestinal epithelial cells. PMID: 26479868
  11. COX-2-derived PGE2 inhibits IL-10 expression in brain microglia through a novel EP2- and beta-arrestin-dependent signaling pathway. PMID: 25218510
  12. A specific hyaluronan-blocking peptide (Pep-1) has confirmed the inflammatory role of degraded hyaluronan as a mediator of the IL-1beta-induced activation of beta-arrestin-1. PMID: 25673209
  13. Data suggest that ARRB1 enhances hepatocellular carcinogenesis by inflammation-mediated Akt signaling. PMID: 26077142
  14. Quantification of beta adrenergic receptor subtypes in beta-arrestin knockout mouse airways. PMID: 25658948
  15. Data show that knockout or knockdown of beta-arrestin-2 (betaarr-2), but not of beta-arrestin-1 (betaarr-1), augments beta adrenoceptor (betaAR)-stimulated cyclic AMP (cAMP) production. PMID: 26103985
  16. a neuroprotective role for ARRB1, in the context of cerebral ischemia, centered on the regulation of BECN1-dependent autophagosome formation PMID: 24988431
  17. results indicate that beta-arrestin1 plays a critical role in the assembly and activation of two major canonical inflammasomes PMID: 25582856
  18. our results reveal a novel and previously unrecognized negative regulatory role of the nonhematopoietic betaArr1 in sepsis-induced inflammation PMID: 24946011
  19. these results suggest that betaarrestin1 regulates rasgrf2 gene expression and Rac activation to affect membrane protrusion and cell migration and invasion. PMID: 24692549
  20. beta-Arrestin-1 mediates the TCR-triggered re-routing of distal receptors to the immunological synapse by a PKC-mediated mechanism. PMID: 24502978
  21. Endothelin-1 promotes podocyte migration via endothelin-A receptor activation and increased beta-arrestin-1 expression. PMID: 24371298
  22. Our findings indicate a novel function for beta1AR-mediated beta-arrestin1 signaling activated by carvedilol in miR biogenesis. PMID: 24334028
  23. betaarr1, via both cardiac and adrenal effects, is detrimental for cardiac structure and function and significantly exacerbates post-myocardial infarction heart failure. PMID: 24218435
  24. ghrelin-induced Akt activity and its downstream targets, the mammalian target of rapamycin complex 1 and the ribosomal protein S6 kinase beta-1, were inhibited by beta-arrestin 1 and 2 siRNAs. PMID: 23557604
  25. study thus demonstrates that beta-arrestin inhibits cell apoptosis through pro-apoptotic ERK1/2 and p38 MAPKs and anti-apoptotic Akt signaling pathways PMID: 22699970
  26. beta-arrestin1 regulates gamma-secretase complex assembly and modulates amyloid-beta pathology PMID: 23208420
  27. Decreased IL-6 production and enhanced IL-10 and IL-22 production in beta-arrestin-1-deficient mice likely lead to attenuated gut inflammation. PMID: 23395087
  28. Pharmacological blockade of a beta(2)AR-beta-arrestin-1 signaling cascade prevents the accumulation of DNA damage in a behavioral stress model. PMID: 23287463
  29. These findings indicate a critical role for beta-arrestin1 in the pathogenesis of collagen-induced arthritis and T(H)17 cell differentiation. PMID: 23589893
  30. Data indicate that beta-arrestin1 is dispensable for STAT1 dephosphorylation and the termination of IFNgamma signaling. PMID: 23582260
  31. analysis of roles of beta-arrestin 1 and beta-arrestin 2 in ORG27569-induced biased signaling and internalization of the cannabinoid receptor 1 PMID: 23449980
  32. PAR(2) has a higher apparent affinity for both beta-arrestins than does NK1R, recruits them at a faster rate, and exhibits more rapid desensitization of the G-protein signal. PMID: 23235155
  33. Findings provide helpful information for clarifying the cold-responsive machinery for beta-arrestin-1 and elucidating low-temperature responses PMID: 22465333
  34. beta-arrestin-1 plays a role in metabolism regulation. PMID: 21543334
  35. Beta-arrestin-1 protein represses adipogenesis and inflammatory responses through its interaction with peroxisome proliferator-activated receptor-gamma (PPARgamma). PMID: 21700709
  36. Studies demonstrate that betaarrestin is a novel Cx43-interacting protein and suggest that, by sequestering betaarrestin, Cx43 facilitates cAMP signaling, thereby exerting a permissive role on osteoblast survival induced by PTH. PMID: 21630325
  37. beta-arrestin 1 and 2 differentially regulate fibroblast-like synoviocytes inflammation and increased beta-arrestin 2 may reduce experimental arthritis severity. PMID: 21855149
  38. examine the different contributions of beta-arrestin1- and beta-arrestin2-mediated regulation of the mu-opioid receptor by comparing MOR agonists in cells that lack expression of individual or both beta-arrestins. PMID: 21757712
  39. results highlight the emerging role of ARRB1 as an E3-ligase adaptor in the nucleus, and reveal how DNA damage may accumulate in response to chronic stress PMID: 21857681
  40. a new urotensin II receptor signalling pathway which is mediated by EGFR trans-activation, dependent by beta-arrestin 1/2, promoting cell survival and cardioprotection. PMID: 21369867
  41. beta-arrestin1 plays a central role in coupling MIF endocytosis to sustained ERK activation PMID: 21283538
  42. These data implicate beta-arrestins 1 and 2 as mediators of fibroblast invasion and the development of pulmonary fibrosis, and as a potential target for therapeutic intervention in patients with idiopathic pulmonary fibrosis. PMID: 21411739
  43. Neurotensin triggers dopamine D2 receptor desensitization through a protein kinase C and beta-arrestin1-dependent mechanism. PMID: 21233215
  44. mitogen-activated protein kinase signaling that was dependent on beta-arrestin-1 and beta-arrestin-2 PMID: 21139074
  45. Data show that Shh induces betaArr1 accumulation and localization to the nucleus, where it participates in enhancing expression of the cyclin dependent kinase (cdk) inhibitor p27, whose accumulation eventually drives CGNP cell cycle exit. PMID: 20935513
  46. The prostaglandin E2 receptor, EP2, stimulates keratinocyte proliferation in mouse skin by G protein-dependent and {beta}-arrestin1-dependent signaling pathways. PMID: 20959465
  47. Nedd4-1 and beta-arrestin-1 as key regulators of NHE1 ubiquitylation, endocytosis, and function. PMID: 20855896
  48. Beta-arr-1 and -2 mediate LPS-induced cytokine secretion in a cell-type specific manner and that both beta-arrestins have overlapping but non-redundant roles in regulating inflammatory cytokine production and endotoxic shock in mice. PMID: 20589830
  49. Studies indicate phosphorylation-independent arrestins as tools for gene therapy. PMID: 20412604
  50. betaarrestin1 and betaarrestin2 collaborate in embryonic development processes for epithelial pneumocyte differentiation and lung maturation. PMID: 20060823

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Subcellular Location
Cytoplasm. Nucleus. Cell membrane. Membrane, clathrin-coated pit. Cell projection, pseudopodium. Cytoplasmic vesicle.
Protein Families
Arrestin family
Database Links
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