Product Pathways - Neuroscience
Arrestin 1/S-Arrestin Antibody #11828
|W||H M R (Mk)||Endogenous||52||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Arrestin 1/S-Arrestin Antibody recognizes endogenous levels of total Arrestin 1/S-Arrestin protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala163 of human Arrestin 1/S-Arrestin protein. Antibodies are purified by protein A and peptide affinity chromatography.
Arrestin proteins function as negative regulators of G protein-coupled receptor (GPCR) signaling. Cognate ligand binding stimulates GPCR phosphorylation, which is followed by binding of arrestin to the phosphorylated GPCR and the eventual internalization of the receptor and desensitization of GPCR signaling (1). Four distinct mammalian arrestin proteins are known. Arrestin 1 (also known as S-arrestin) and arrestin 4 (X-arrestin) are localized to retinal rods and cones, respectively. Arrestin 2 (also known as β-arrestin 1) and arrestin 3 (β-arrestin 2) are ubiquitously expressed and bind to most GPCRs (2). β-arrestins function as adaptor and scaffold proteins and play important roles in other processes, such as recruiting c-Src family proteins to GPCRs in Erk activation pathways (3,4). β-arrestins are also involved in some receptor tyrosine kinase signaling pathways (5-8). Additional evidence suggests that β-arrestins translocate to the nucleus and help regulate transcription by binding transcriptional cofactors (9,10).
Arrestin 1/S-Arrestin inactivates rhodopsin-mediated signaling through binding to the light-activated phosphorylated rod photoreceptor, thereby preventing coupling to transducin, rhodopsin's cognate G protein (11). Research studies have proposed that mutations in the Arrestin 1/S-Arrestin gene are linked to Oguchi disease (12,13) and Retinitis Pigmentosa (14).
- Shenoy, S.K. and Lefkowitz, R.J. (2005) Sci STKE 2005, cm10.
- Lefkowitz, R.J. and Shenoy, S.K. (2005) Science 308, 512-7.
- Luttrell, L.M. et al. (1999) Science 283, 655-61.
- Luttrell, L.M. et al. (1999) Curr Opin Cell Biol 11, 177-83.
- Luttrell, L.M. and Lefkowitz, R.J. (2002) J Cell Sci 115, 455-65.
- Waters, C. et al. (2004) Semin Cell Dev Biol 15, 309-23.
- Lefkowitz, R.J. and Whalen, E.J. (2004) Curr Opin Cell Biol 16, 162-8.
- Waters, C.M. et al. (2005) Cell Signal 17, 263-77.
- Kang, J. et al. (2005) Cell 123, 833-47.
- Ma, L. and Pei, G. (2007) J Cell Sci 120, 213-8.
- Gurevich, V.V. et al. (2011) Prog Retin Eye Res 30, 405-30.
- Yamada, T. et al. (1999) Ophthalmic Genet 20, 117-20.
- Waheed, N.K. et al. (2012) Mol Vis 18, 1253-9.
- Nakazawa, M. et al. (1998) Arch Ophthalmol 116, 498-501.
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For Research Use Only. Not For Use In Diagnostic Procedures.