Rhodopsin Epitope Tag

Rhodopsin Epitope Tag is a 9-amino acid peptide localized within the C-terminal region of bovine rhodopsin . Rhodopsin Epitope Tag is widely used as an epitope tag and can be recognized by a number of anti-rhodopsin antibodies.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R1660

Synonyms/Alias:Rhodopsin Epitope Tag;102099-07-0;EX-A9662;HY-P1509;Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala;MS-31683;CS-0044605;G13700;(4S)-5-[[(2S,3R)-1-[[(2S)-1-[[(2S)-5-amino-1-[[(2S)-1-[[(2S)-1-[(2S)-2-[[(1S)-1-carboxyethyl]carbamoyl]pyrrolidin-1-yl]-1-oxopropan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-4-[[(2S,3R)-2-amino-3-hydroxybutanoyl]amino]-5-oxopentanoic acid

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cGMP Peptide
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  • CMC information required for an IND
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  • Drug master files (DMF) filing
M.F/Formula
C₃₇H₆₂N₁₀O₁₆
M.W/Mr.
902.95
Sequence
One Letter Code: TETSQVAPA
three Letter Code: Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala

Rhodopsin Epitope Tag is a synthetic peptide sequence derived from the C-terminal region of bovine rhodopsin, widely utilized as an affinity tag in molecular biology and biochemical research. As a versatile peptide reagent, it enables the specific labeling, detection, and purification of recombinant proteins through its recognized epitope, typically targeted by high-affinity monoclonal antibodies. Due to its compact size and minimal impact on protein structure or function, the rhodopsin tag has become an established tool for facilitating a range of experimental workflows in protein engineering, cellular biology, and proteomics. Its integration into fusion proteins streamlines downstream analysis while maintaining the native characteristics of the protein of interest, making it highly relevant for diverse research applications.

Protein Detection: The rhodopsin epitope sequence is frequently incorporated into recombinant proteins to allow sensitive and selective detection using anti-rhodopsin antibodies. This approach is particularly valuable in Western blotting, immunocytochemistry, and immunofluorescence assays, where the tag provides a consistent and well-characterized antigenic determinant. By enabling precise visualization of tagged proteins in complex biological samples, the epitope facilitates studies of protein expression, localization, and dynamics within various cellular contexts.

Affinity Purification: Incorporation of the rhodopsin tag into target proteins supports highly specific purification strategies based on immunoaffinity chromatography. The tag's strong and selective interaction with immobilized rhodopsin antibodies permits efficient capture and elution of fusion proteins from cell lysates or tissue extracts. This method streamlines the isolation of recombinant proteins under native or denaturing conditions, minimizing contamination from endogenous proteins and simplifying downstream analytical workflows.

Protein-Protein Interaction Studies: The rhodopsin tag serves as a reliable handle for co-immunoprecipitation and pull-down assays, enabling researchers to investigate the binding partners and interaction networks of tagged proteins. By using anti-tag antibodies to selectively isolate the protein complex of interest, it becomes possible to unravel molecular associations, map signaling pathways, and identify novel interactors with high specificity. This application is fundamental for dissecting cellular processes and elucidating mechanistic details in systems biology.

Live Cell Imaging: The small size and immunogenicity of the rhodopsin tag make it suitable for live cell imaging applications when combined with fluorescently labeled antibodies or nanobodies. Tagging proteins with the epitope allows real-time visualization of protein trafficking, subcellular localization, and dynamic interactions in living cells. This capability is essential for studying temporal and spatial regulation of protein function, as well as monitoring responses to experimental perturbations in a physiologically relevant environment.

Quality Control in Protein Production: The rhodopsin epitope tag is also employed in the quality assessment of recombinant protein expression systems. By enabling rapid detection and quantification of tagged proteins during various stages of production, it aids in optimizing expression conditions, verifying product integrity, and monitoring batch consistency. The use of this tag thus supports robust process development and analytical validation in research-scale and pre-commercial protein manufacturing workflows.

Length
9

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