Product Description | The peptide sequence ENLYFQ is a recognition sequence for the Tobacco Etch Virus (TEV) protease, which is a highly specific cysteine protease widely used in biotechnology. This enzyme cleaves precisely at the ENLYFQS site, where the scissile bond is between Q (glutamine) and S (serine). Though serine (S) is the most efficient residue in the P1’ position (immediately following the Q), the sequence can also tolerate glycine (G), alanine (A), methionine (M), cysteine (C), or histidine (H) without a significant drop in activity. TEV protease’s specificity makes it ideal for removing affinity tags like maltose-binding protein (MBP) or poly-histidine tags, which are frequently used in recombinant protein purification. Because of its high precision, TEV protease can minimize unintended cleavage in the target protein. After digestion, the TEV protease itself can be easily removed from the reaction using its 7xHis-tag, which binds to nickel affinity resins, simplifying the purification of the cleaved protein product. Additionally, engineered versions of TEV protease have been developed to enhance thermal stability and reduce autolysis, which improves its utility in a variety of laboratory conditions. These modifications help to maintain enzymatic activity over a broader range of temperatures, making it suitable for diverse protein purification workflows in research and therapeutic applications? |
Scientific Background | TEV protease cleavage sequence ENLYFQ is a 13-residue synthetic peptide with the sequence Gly-Ser-Gly-Ser-Glu-Asn-Leu-Tyr-Phe-Gln-Ser-Gly-Ser. Biotin provides an affinity handle for streptavidin-based capture or detection. These sequence-derived properties describe the reagent chemically; no specific receptor, enzyme, pathway, disease association, or biological activity is assigned without product-specific experimental evidence. |
Experimental Notes | Sequence-derived chemical properties support reagent selection and experimental planning but do not establish biological function. Solubility, aggregation, adsorption, conjugation efficiency, and assay performance should be validated under the intended experimental conditions. |
