Acts as a (oligo)glycine nucleophile in the final steps of a sortagging reaction, which results in a NIR emitting fluorescent dye being attached to the C-terminus of target peptide.
Catalogue number crb1101496 Molecular Weight 1121.4 Sequence (one letter code)
Sequence (three letter code)
Purity >95% Storage -20°C References
Strijbis et al (2012) Protein Ligation in Living Cells Using Sortase. Traffic 13(6) 780 PMID: 22348280
Sinisi et al (2012) Development of an Influenza virus Protein Array Using Sortagging Technology. Bioconjug. Chem. 23(6) 1119 PMID: 22594688
Ton-That et al (2000) Anchoring of Surface Proteins to the Cell Wall ofStaphylococcus aureus. J. Biol. Chem. 275(13) 9876 PMID: 10734144
Manufactured in: United Kingdom
This C-terminal Sortagging peptide acts as a (oligo)glycine nucleophile in the final steps of a sortagging protein labelling reaction. This reaction results in the (Sulfocyanine7) fluorescent moiety being attached to the C-terminus of the target protein or peptide.
A substrate peptide containing the LPXTG motif 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 of the substrate peptide. Cleavage results in the formation of a thioacyl intermediate between the substrate peptide and SrtA. This intermediate is then resolved by the N-terminus of this (oligo)glycine nucleophile peptide, resulting in the creation of a new peptide bond that links the substrate peptide to this peptide and its fluorescent dye. This method of protein labelling is known as sortagging.
This peptide contains Sulfocyanine7, which is a NIR (near infrared) emitting fluorescent dye.