Arrestin, beta 1 (ARRB1) (AA 262-409) antibody

Details for Product No. ABIN968033
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Synonyms arrb1, MGC83787, arb1, arr1, barr1, betaarr1, 1200006I17Rik, AW208571, G430100A01Rik, ARB1, ARR1, BARRES
AA 262-409
(27), (19), (15), (6), (5), (3), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1)
Rat (Rattus)
(95), (35), (30), (2), (1)
(83), (14), (2)
Clonality (Clone)
Monoclonal ()
(3), (3), (3), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1)
Western Blotting (WB)
(87), (40), (36), (30), (19), (14), (10), (10), (5), (3), (3), (3), (1), (1)
Pubmed 5 references available
Quantity 150 μg
Shipping to United States (Change)
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Catalog No. ABIN968033
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Immunogen Rat beta-Arrestin1
Clone 4B9
Isotype IgG1
Cross-Reactivity Mouse (Murine), Human
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name beta-Arrestin1
Background Beta-Arrestins were discovered due to their ability to modulate interactions between the phosphorylated beta2-Adrenergic receptors and G proteins. This modulation results in diminished beta2-Adrenergic receptor function, also known as desensitization. Because CoA and C27-bile acyl-CoAs to their (S)-stereoisomers, which are the only stereoisomers degraded by peroxisomal alpha-oxidation. Interestingly, AMACR mutations have been linked to some sensory motor neuropathies where accumulation of fatty acids and AMACR deficiencies correlate with pathogenesis. AMACR contains an N-terminal region required for mitochondrial localization, and a C-terminal peroxisomal targeting signal type 1 (PTS). AMACR mRNA is expressed preferarrestins are found at the synaptic terminals, they may provide a termination mechanism that allows the neurons to regain their original polarization and respond to a new neurotransmitter stimulus. The C-terminal region of arrestins is involved in selecting the phosphorylated and activated adrenergic receptors. The beta-Arrestin1 gene encodes a protein of 418 amino acids with an approximate molecular weight of 55kDa. beta-Arrestin1 protein is highly homologous to the 45kDa beta-Arrestin2. Both proteins are widely expressed, but are especially abundant in the central nervous system.
This antibody is routinely tested by western blot analysis of AMACR enzymatic activity found in the mitochondria relative to the peroxisomes differs depending on the species. Thus, AMACR is an enzyme critical for fatty acid degradation, and bile formation.
Molecular Weight 55 kDa

Related Products: ABIN968555, ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
anti-Arrestin, beta 1 (ARRB1) (AA 262-409) antibody Western blot analysis of beta-Arrestin on a mouse macrophage lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of the anti- beta-Arrestin antibody.
anti-Arrestin, beta 1 (ARRB1) (AA 262-409) antibody (2) anti-Arrestin, beta 1 (ARRB1) (AA 262-409) antibody (Image 2)
Product cited in: Dalle, Imamura, Rose et al.: "Insulin induces heterologous desensitization of G-protein-coupled receptor and insulin-like growth factor I signaling by downregulating beta-arrestin-1." in: Molecular and cellular biology, Vol. 22, Issue 17, pp. 6272-85, 2002 (PubMed).

Imamura, Huang, Dalle et al.: "beta -Arrestin-mediated recruitment of the Src family kinase Yes mediates endothelin-1-stimulated glucose transport." in: The Journal of biological chemistry, Vol. 276, Issue 47, pp. 43663-7, 2001 (PubMed).

DeFea, Zalevsky, Thoma et al.: "beta-arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2." in: The Journal of cell biology, Vol. 148, Issue 6, pp. 1267-81, 2000 (PubMed).

Gurevich, Dion, Onorato et al.: "Arrestin interactions with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, beta 2-adrenergic, and m2 muscarinic cholinergic receptors." in: The Journal of biological chemistry, Vol. 270, Issue 2, pp. 720-31, 1995 (PubMed).

Attramadal, Arriza, Aoki et al.: "Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family." in: The Journal of biological chemistry, Vol. 267, Issue 25, pp. 17882-90, 1992 (PubMed).

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