Rho 1D4 Antibody

Dr. Robert Molday and coworkers at The University of British Columbia, have developed a cell line for the Rho 1D4 antibody and have isolated and characterized the epitope sequence in Rho 1D4 (9 amino acids). The antibody can be covalently bound to affinity gels directly using cyanogen bromide or indirectly using any of the common immobilization linkers. The antibody specifically binds to the C- terminal epitope -T-E-T-S-Q-V-A-P-A- (COOH) of rhodopsin. Proteins containing the epitope tag can be selectively bound to a Rho 1D4 affinity matrix and eluted using an excess of -T-E-T-S-Q-V-A-P-A- peptide under mild conditions. Advantages:
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Can be used for the development of protein expression and purification systems
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Can be used for the detection of 1D4-tagged proteins using immunocytochemical (e.g. immmunofluorescence labeling for conventional and confocal microscopy, and immunogold labeling for transmission and electron microscopy) or western blotting techniques.
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Can be used for co- immunoprecipitation studies to analyze subunit interactions and protein-protein interactions.
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Can be used for purification of 1D4-epitope-tagged proteins for structure-function analysis.
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Can be used for direct analysis of the cellular and subcellular distribution of rhodopsin and for structure-function studies.

Type of Offer: Licensing



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