S-Arrestin (SAG, S-AG, 48kD Protein, Retinal S-antigen, Rod Photoreceptor Arrestin)

The arrestin proteins are a family of regulators of cell signaling of G protein-coupled receptors (GPCR). Visual arrestin was first discovered as a result of the experimental model of human uveitis, an autoimmune disease of the eye. In this model, called experimental allergic uveitis, animals were injected with extracts made from the retina of the same species mixed with Freund's complete adjuvant. The animals mounted a strong immune response to the extract, and the antibody response was used to identify several immunogenic retinal proteins. One of these was called S-antigen, for soluble antigen. The protein was found to be abundant in retina, about 48kD in molecular weight, and localized in the outer segments of the photoreceptors (1, 2). Several years later, Hermann K

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SPECIFICATIONS

Catalog Number

031426

Size

100ul

Applications

IF, WB

Hosts

Mouse

Reactivities

Hum, Rat, Bov, Prc

Form

Supplied as a liquid in PBS, 10mM sodium azide.

P Type

Mab

Purity

Purified by Protein G affinity chromatography.

Isotype

IgG1,k

References

1. Dorey C, Faure JP. [Isolation and characterization of a retinal antigen inducing experimental autoimmune uveo-retinitis]. [Article in French] Ann Immunol (Paris). 128:229-32 (1977).\n\n2. Wacker WB, Donoso LA, Kalsow CM, Yankeelov JA Jr, Organisciak DT. Experimental allergic uveitis. Isolation, characterization, and localization of a soluble uveitopathogenic antigen from bovine retina. J Immunol. 119:1949-58 (1977).\n\n3. KГјhn H, Hall SW, Wilden U. Light-induced binding of 48-kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsin. FEBS Lett. 176:473-8 (1984).\n\n4. Pfister C, Chabre M, Plouet J, Tuyen VV, De Kozak Y, Faure JP, KГјhn H. Retinal S antigen identified as the 48K protein regulating light-dependent phosphodiesterase in rods. Science 228:891-3 (1985).\n\n5. Wilden U, Hall SW, KГјhn H. Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments. Proc Natl Acad Sci USA 83:1174-8 (1986).\n\n6. Lohse MJ, Benovic JL, Codina J, Caron MG, Lefkowitz RJ. b-arrestin: a protein that regulates beta-adrenergic receptor function. Science 248: 1547-1550 (1990).\n\n7. Smith WC, Mc Dowell JH, Dugger DR, Miller R, Arendt A, Popp MP, Hargrave PA. Identification of regions of arrestin that bind to rhodopsin. Biochemistry 38:2752-61 (1999).

Additional Info

Recognizes visual Arrestin from human, bovine, mouse, porcine and rat. Does not bind the other three arrestin molecules. In the retina this antibody binds to rod cell bodies and rod outer seqments. The arrestin protein runs at about ~48kD on SDS-PAGE gels.