Western Blot: S-arrestin Antibody (S128) [NBP2-25161] - Blot of bovine retinal extracts. The antibody stains a band corresponing to S-arrestin at about 48 kDa.
Immunocytochemistry/ Immunofluorescence: S-arrestin Antibody (S128) [NBP2-25161] - Confocal image of a pig retina stained with NBP2-25161 (green). S-arrestin is most abundant in the outer segments (OS) and inner surface ...read more
Use in Immunohistochemistry-Frozen reported in scientific literature (PMID:35024589).This S-arrestin (S128) antibody is useful for Immunocytochemistry/Immunofluorescence and Western Blot, where a band can be seen at ~48 kDa..
Theoretical MW
48 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publication using NBP2-25161 in the following applications:
Use in Rat reported in scientific literature (PMID:35024589) .
Packaging, Storage & Formulations
Storage
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
Buffer
50% PBS, 50% glycerol
Preservative
5mM Sodium Azide
Concentration
1 mg/ml
Purity
Protein G purified
Alternate Names for S-arrestin Antibody (S128) - BSA Free
arrestin 1
RP47,48 kDa protein
S-antigen; retina and pineal gland (arrestin)
S-arrestin
visual arrestin
Background
Arrestin proteins are a family of regulators of cell signaling of G protein-coupled receptors (GPCR). S-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 48 kDa in molecular weight, and localized in the outer segments of the photoreceptors. Several years later, Hermann Kuhn and colleagues discovered that this protein binds to phosphorylated Rhodopsin and prevents this protein from activating transducin. Transducin is a typical heterotrimeric G protein, composed of alpha and beta gamma subunits. Rhodopsin phosphorylation is mediated by Rhodopsin kinase (a.k.a. GRK1), the prototypic member of a family of GPCR kinases. Since the S-antigen protein arrested the activity of Rhodopsin it was renamed S-arrestin, and became the prototypic member of the arrestin protein family. Subsequently, Robert Lefkowitz and colleagues discovered a related protein which bound to phosphorylated beta-adrenergic GPCRs and prevented these proteins from activating their specific heterotrimeric G proteins. Because of this relationship to the beta-adrenergic receptor and functional and structural similarities to S-arrestin this protein was named beta-arrestin. The beta-adrenergic receptor was phosphorylated by the beta-adrenergic receptor kinase (a.k.a. GRK2), an enzyme belonging to GPCR kinase family. Studies of visual transduction therefore aided greatly in understanding other kinds of GPCR signaling. In mammals, there are four arrestin isoforms; S-arrestin (a.k.a. S-antigen, visual arrestin and arrestin-1) and cone arrestin (a.k.a. arrestin-4) are largely confined to photoreceptors. Beta-arrestin 1 (a.k.a. arrestin 2) and beta-arrestin-2 (a.k.a. arrestin-3) are ubiquitous and regulate non-visual GPCRs.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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