Monoclonal Anti-Rhodopsin antibody produced in mouse

Vision involves the conversion of light into electrochemical signals that are processed by the retina and subsequently sent to and interpreted by the brain. The process of converting light to an electrochemical signal begins when the membrane-bound protein, rhodopsin, absorbs light within the retina. Photoexcitation of rhodopsin causes the cytoplasmic surface of the protein to become catalytically active. In the active state, rhodopsin activates transducin, a GTP binding protein. Once activated, transducin promotes the hydrolysis of cGMP by phosphodiesterase (PDE). The decrease of intracellular cGMP concentrations causes the ion channels within the outer segment of the rod or cone to close, thus causing membrane hyperpolarization and, eventually, signal transmission. Rhodopsin′s activity is believed to be shut off by its phosphorylation followed by binding of the soluble protein arrestin.

bovine rhodopsin.

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)

Mouse monoclonal clone 1D4 anti-Rhodopsin antibody has been successfully used in Western blot, immunocytochemistry, and immunoprecipitation. It is used as a probe to determine the presence and roles of rhodopsin in the conversion of light into electrochemical signals.

By Western blot, mouse monoclonal clone 1D4 anti-Rhodopsin antibody detects an ~40 kDa protein representing rhodopsin from Sf 9 cells expressing the bovine gene. Immunocytochemical staining of rhodopsin in human retinal samples results in staining of both rod and cone outer segments.

The epitope for this antibody has been localized to the C-terminal nine amino acids of bovine rhodopsin known as the 1D4 epitope, and detects rhodopsin from human and bovine retinal samples.

Solution in phosphate buffered saline containing 1 mg/mL BSA and 0.05% sodium azide.

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