Sortase reagents

Protein-sorting transpeptidases are enzymes that cleave target proteins produced by the same cell, as part of a specialized pathway of protein targeting.  Protein-sorting transpeptidases transfer the N-terminal portion of the cleaved polypeptide into another molecule. The term sortase is correctly reserved for the cysteine protease enzymes sortase A, sortase B, and members of additional classes, all of which share homology.

We now offer the sortase recognition sequence, LPETGG, coupled to the fluorescent labels 5-FAM, Atto488, Atto550 and Atto647N, which can be used for site-specific labeling of target proteins using sortase-catalyzed transpeptidation. Sortase A cleaves between the thr and gly residues, forming a thioester intermediate with the peptide probe. A protein N-terminally engineered with a series of glycine residues resolves this intermediate, regenerating the active site cysteine of sortase and conjugating the probe to the N-terminus of the protein. Our fluorescent labelled LPETGG derivatives are efficiently excited in ranges between 480 - 660 nm, with strong absorption, high fluorescence quantum yield and high photo-stability. Other labels can be added on request.

View the range here : https://www.iscabiochemicals.com/products/205/126