Rabbit polyclonal primary
Beta-Arrestin 1 Antibody (ER1802-13)
Human placenta tissue lysate, A549, HUVEC, LOVO, rat brain tissue, human colon cancer tissue, human breast tissue, mouse colon tissue, Jurkat.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Peptide affinity purified
ARB1 antibody; ARR1 antibody; ARRB1 antibody; ARRB1_HUMAN antibody; Arrestin 2 antibody; Arrestin beta 1 antibody; Arrestin beta-1 antibody; Beta-arrestin-1 antibody
Belongs to the arrestin family.
Constitutively phosphorylated at Ser-412 in the cytoplasm. At the plasma membrane, is rapidly dephosphorylated, a process that is required for clathrin binding and ADRB2 endocytosis but not for ADRB2 binding and desensitization. Once internalized, is rephosphorylated.; The ubiquitination status appears to regulate the formation and trafficking of beta-arrestin-GPCR complexes and signaling. Ubiquitination appears to occur GPCR-specific. Ubiquitinated by MDM2; the ubiquitination is required for rapid internalization of ADRB2. Deubiquitinated by USP33; the deubiquitination leads to a dissociation of the beta-arrestin-GPCR complex. Stimulation of a class A GPCR, such as ADRB2, induces transient ubiquitination and subsequently promotes association with USP33.
Cytoplasm. Membrane. Nucleus.
The members of the G protein coupled receptor family are distinguished by their slow transmitting response to ligand binding. These seven transmembrane proteins include the adrenergic, serotonin and dopamine receptors. The effect of the signaling molecule can be excitatory or inhibitory depending on the type of receptor to which it binds. Members of the β-Arrestin family regulate receptor binding to G proteins. β-Arrestins have been found to be located at postsynaptic sites, where they are thought to act in concert with βARK (βARK1, also designated GRK 2, or βARK2, also designated GRK 3) to regulate G protein-coupled neurotransmitter receptors. Expression of β-Arrestin-1 and b-Arrestin-2 is seen predominantly in spleen and neuronal tissues. It has been shown that β-Arrestin-1 expression is modulated by intracellular cAMP, which may be a novel mechanism for the regulation of receptor-mediated responses.