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Pyroglutamate aminopeptidase is a cysteine peptidase that cleaves pyroglutamic acid (pGlu) from the N-terminus of proteins and peptides.1 It is specific for L-pGlu-L-amino acid isomers and does not typically cleave pGlu-Pro bonds. Pyroglutamate aminopeptidase has been found in various species, including bacteria, mammals, fish, and birds and exists as a multimer in bacteria.1,2 Pyroglutamate aminopeptidase has commonly been used to remove pGlu from the N-terminus of peptides and proteins prior to Edman degradation and sequencing.3 Cayman’s Pyroglutamate Aminopeptidase (P. furiosus, recombinant) protein can be used for Edman degradation and protein sequencing applications.
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1. Pyroglutamyl peptidase: An overview of the three known enzymatic forms. Biochim. Biophys. Acta 1429(1), 1-17 (1998).
2. Pyroglutamyl-
3. High-