Technical Data
Arrestin 1, beta, phosphorylated (Ser412) (ARRB1, ARB1, ARR1)
Beta arrestin-1 is a member of a family of proteins widely expressed but especially abundant in the central nervous system. Serving as an adaptor or scaffold molecule, b-arrestin-1 is essential for mitogenic signaling and mediates agonist-dependent desensitization and internalization of G protein-coupled receptors (GPCRs, e.g., b2-adrenergic receptor). After binding to their ligand and interacting with heterotrimeric G proteins, GPCRs are phosphorylated by G-protein receptor kinases (GRKs) on serine residues. b-arrestin-1 in the cytosol is phosphorylated by ERK1&2 on serine 412 in a negative feedback mechanism and binds to the phosphorylated receptors at the plasma membrane. Serine 412 is then dephosphorylated and the GPCRs are internalized, leading to activation of the Ras Raf ERK1&2 signaling pathway.

Suitable for use in ELISA, Western Blot, Immunoprecipitation, Immunohistochemistry, Immunocytochemistry. Other applications not tested.

Recommended Dilution:
Western Blot: 0.1-1ug/ml
Optimal dilutions to be determined by the researcher.

Positive Control:
PC12 and CHO-K cells

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
PabIgGAffinity Purified
100ul-20CBlue IceRatRabbit
Not determined
Synthetic phosphopeptide corresponding to rat b-arrestin-1 that contains serine 412.
Purified by immunoaffinity chromatography.
Supplied as a liquid in PBS (without Mg2+ and Ca2+), 1mg/ml BSA (IgG, protease free), pH 7.2, 0.05% sodium azide.
Recognizes mouse and rat b-arrestin-1 when phosphorylated at Ser412. Species sequence homology: human and bovine (77%) b-arrestin-1 have not been tested, but are expected to react.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Tohgo, A., et al. (2002) beta-Arrestin scaffolding of the ERK cascade enhances cytosolic ERK activity but inhibits ERK-mediated transcription following angiotensin AT1a receptor stimulation. J. Biol. Chem. 277(11):9429-9436. 2. Miller, W.E., et al. (2000) beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis. J. Biol. Chem. 275(15):11312-11319. 3. Lefkowitz, R.J. (1998) G protein-coupled receptors. III. New roles for receptor kinases and betaarrestins in receptor signaling and desensitization. J. Biol. Chem. 273(30):18677-18680.