Mouse RHO Monoclonal Antibody | anti-RHO antibody

RHO Antibody

Cat. Num. AAA415194

• Reactivity: Human, bovine, mouse, pig and rat
• Applications: Immunofluorescence, Western Blot
• Purity: Affinity purified
• Synonyms: RHO; Monoclonal Antibody; RHO Antibody; anti-RHO antibody

• Host: Mouse
• Reactivity: Human, bovine, mouse, pig and rat
• Clonality: Monoclonal
• Isotype: IgG1
• Purity/Purification: Affinity purified
• Form/Format: Liquid
• Concentration: 100ug/100ul (varies by lot)

• Applicable Applications for anti-RHO antibody: Immunofluorescence (IF), Western Blot (WB)
• Application Notes: Try at dilutions of ~1:1,000 for immunofluorescence. For western blots try at 1:5,000.
• Immunogen: Rhodopsin is the protein in the mammalian retina responsible for the light sensitivity of rod cells, which are responsible for vision in low light levels. Somewhat surprisingly, the rhodopsin protein turned out to be a typical member of the seven transmembrane G protein-coupled receptor (GPCR) superfamily. Whereas other GPCRs initiate signaling on binding a specific ligand, rhodopsin exists with a ligand already bound, specifically the vitamin A related substance retinal. Retinal can exist in two isomeric forms, 11-cis and 11-trans retinal. In the dark rhodopsin is associated with 11-cis retinal, but photons cause the 11-cis form to flip to the 11-trans form, and this causes an alteration in the structure of the rhodopsin making it catalytically active. Activated rhodopsin in turn activates the GTP binding protein transducin by favoring the loss of GDP and the addition of GTP. Transducin is a typical member of the family of heterotrimeric G proteins, and consists of an α and a betagamma subunit. The α subunit is responsible for the GTP binding and the GTP bound form activates a phosphodiesterase (PDE) enzyme which hydrolyses cyclic GMP. This in turn results in the closure of cyclic nucleotide gated ion channels in the rod cell membrane, which prevent the influx of sodium and calcium ions. This results in an increase in the membrane potential of the rod cell and so reduces the rate of synaptic signaling. So light stimulation results in a reduced rate of photoreceptor synaptic release. This information is transmitted through neurons of the retina to the visual centers of the brain (see review 1, 2). Rhodopsin activity is shut off by phosphorylation under the influence of rhodopsin kinase, the activity of which results in binding of visual arrestin, which prevents rhodopsin from interacting with and activating more transducin molecules (3, 4). This basic signaling paradigm proved to be a prototype for understanding how other GPCRs function, as proteins similar to transducin, arrestin and rhodopsin kinase are found in these pathways. MCA-B630 was raised against bovine outer segment discs and shows convincing staining for rhodopsin both on western blots and on sections of retina. The protein is concentrated in rod outer segments. The HGNC name for this protein is RHO.
• Storage Buffer: PBS, pH 7.4 with 0.02% sodium azide.
• Preparation and Storage: Store at -20 degree C/1 year

Western Blot (WB)

References

1. Molday RS. Photoreceptor membrane proteins, phototransduction, and retinal degenerative disease. The Frienwald lecture. Invest Ophthalmol Vis Sci. 39:2491-513 (1998).2. Yau KW. Phototransduction Mechanism in Retinal Rods and Cones. The Frienwald lecture. Invest Ophthalmol Vis Sci. 35:9-32 (1994).3. Wilden U, Hall SW, Kohn 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).4. 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).