TEV protease is widely used in molecular biology and protein engineering for its high specificity in cleaving peptide bonds. It is commonly employed in the removal of affinity tags from recombinant fusion proteins during purification processes. Due to its stringent recognition sequence (Glu-Asn-Leu-Tyr-Phe-Gln↓Ser/Ala/Gly), TEV protease minimizes non-specific cleavage, making it ideal for precise protein manipulation. It is especially valuable in structural biology and proteomics workflows where obtaining a native protein sequence is critical. The enzyme functions efficiently at 4–30°C and in a variety of buffer conditions, allowing integration into different purification systems. Its activity can be easily controlled, and mutant versions are available for enhanced stability or altered cleavage kinetics. TEV protease is often used in high-throughput protein production pipelines and in the preparation of samples for crystallography, NMR, or functional assays.