[5-TAMRA]-LPETAG N-terminal Sortagging - Fluorescent Peptides

This peptide is recognised and cleaved by the enzyme Sortase A (SrtA) from-Staphylococcus aureus. The catalytic cysteine residue in the active site of SrtA, serves as a nucleophile to cleave the peptide bond between threonine and glycine. Cleavage results in the formation of a thioacyl intermediate between the peptide and SrtA. This intermediate is then resolved by the N-terminus of an (oligo)glycine nucleophile, resulting in the creation of a new peptide bond that links the peptide and its-nucleophile, resulting in the creation of a new peptide bond that links the peptide and its fluorescent- to the incoming nucleophile.- This method of protein labelling is known as sortagging 5-Carboxytetramethylrhodamine (5-TAMRA) is a widely used fluorescent dye which excites at 546 nm and emits at 579 nm