C-terminal Sortagging-[Cys(Sulfocyanine5)]
GGG-[C(Sulfocyanine5)]-amide
Description
Application Data
Description
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Acts as a (oligo)glycine nucleophile in the final steps of a sortagging reaction, which results in the red fluorescent dye being attached to the C-terminus of the target peptide.
Application Data
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Data Sheet Material Safety Data Sheet (MSDS)Catalogue number crb1101487 Molecular Weight 1055.4 Sequence (one letter code) GGG-[C(Sulfocyanine5)]-amide
Sequence (three letter code) H-Gly-Gly-Gly-[Cys(Sulfocyanine5)]-NH2
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 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 Sulfocyanine5, which is a fluorescent red dye.
C-terminal Sortagging-[Cys(Sulfocyanine5)]
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