Pfu Pyroglutamate Aminopeptidase liberates the N-terminal pyroglutamic acid from proteins and peptides. This enzyme may work well with some intact, non-denatured protein. In such cases, a denaturation step may be unnecessary. This product is supplied with 5X Reaction Buffer [250 mM sodium phosphate (pH 7.0), 50 mM DTT, 5 mM EDTA].
Applications
Removal of pyroglutamic acids from the N-termini of proteins and peptides
Components
Supplied Buffer
Volume: 1 ml
Component: 250 mM sodium phosphate buffer (pH 7.0) containing 50 mM DTT and 5 mM EDTA
Comparison of specific activities across different temperatures: 5.83 U/mg protein at 37°C showed activities of 12.2 U/mg protein or 28.3 U/mg protein at 50°C or 75°C, respectively.
Source
Recombinant Escherichia coli encoding the Pyrococcusfuriosuspyroglutamate aminopeptidase gene.
Purity
Greater than or equal to 90% via SDS-PAGE. No other protease activity detected.
Hamazume, Y. & Mega, T. Positions of Disulfide Bonds in Riboflavin-Binding Protein of Hen Egg White. J. Biochem101, 217–223 (1987).
Shimada, Y., Sugihara, a, Tominaga, Y., Iizumi, T. & Tsunasawa, S. cDNA molecular cloning of Geotrichum candidum lipase. J. Biochem.106, 383–388 (1989).
Pfu Pyroglutamate Aminopeptidase liberates the N-terminal pyroglutamic acid from proteins and peptides. This enzyme may work well with some intact, non-denatured protein. In such cases, a denaturation step may be unnecessary. This product is supplied with 5X Reaction Buffer [250 mM sodium phosphate (pH 7.0), 50 mM DTT, 5 mM EDTA].
Applications
Removal of pyroglutamic acids from the N-termini of proteins and peptides
Components
Supplied Buffer
Volume: 1 ml
Component: 250 mM sodium phosphate buffer (pH 7.0) containing 50 mM DTT and 5 mM EDTA
Comparison of specific activities across different temperatures: 5.83 U/mg protein at 37°C showed activities of 12.2 U/mg protein or 28.3 U/mg protein at 50°C or 75°C, respectively.
Source
Recombinant Escherichia coli encoding the Pyrococcusfuriosuspyroglutamate aminopeptidase gene.
Purity
Greater than or equal to 90% via SDS-PAGE. No other protease activity detected.
Hamazume, Y. & Mega, T. Positions of Disulfide Bonds in Riboflavin-Binding Protein of Hen Egg White. J. Biochem101, 217–223 (1987).
Shimada, Y., Sugihara, a, Tominaga, Y., Iizumi, T. & Tsunasawa, S. cDNA molecular cloning of Geotrichum candidum lipase. J. Biochem.106, 383–388 (1989).