This mouse IgG1k monoclonal antibody was generated against human ß-arrestin-1 and recognizes human, rat, and hamster beta- arrestin 1 or beta-arrestin 2.
Beta-arrestins function 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. Arrestin binding to the receptor blocks further G protein-mediated signaling and targets receptors for internalization, and redirects signaling to alternative G protein-independent pathways, such as ß-arrestin signaling. In addition to GPCRs, arrestins bind to other classes of cell surface receptors and a variety of other signaling proteins.
From the laboratory of Martin Oppermann, MD, University Medical Center Götingen.
|Antigen:||Human and rat ß-arrestin-1; ß-arrestin-2|
|Reactivity:||Reacts equally well with (human, rat and hamster) beta- arrestin1 or beta-arrestin2; other species not tested|
|Species Immunized:||Mouse (Balb/c)|
|Buffer:||0.1M Sodium Phosphate, pH 7.4, 0.15M NaCl, 0.05% (w/v) Sodium Azide|
|Tested Applications:||WB, IP|
Immunoblots showing the specificity of anti beta-arrestin1/2 mAb 21-B1. Left: Cell lysates from HEK-293 cells overexpressing either rat beta-arrestin1 (A) or rat beta-arrestin2 (B) were probed with 21-B1 and two other mAb specific for beta-arrestin1 (7-F3 and 25-G10). Right: C5a-induced translocation of endogenous beta-arrestin1/2 from the cytosol (Cyt) to the plasma membrane (Mem) in the human myelo-monocytic cell line U937.
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