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Edman degradation and protein sequencing: Pfu Pyroglutamate Aminopeptidase

Pfu Pyroglutamate Aminopeptidase removes pyroglutamic acids from the N-termini of proteins and peptides, enabling protein sequencing following Edman degradation.

This enzyme may work well with some intact and non-denatured proteins; a denaturation step may be unnecessary in some cases. Pfu Pyroglutamate Aminopeptidase is supplied with a 5X Reaction Buffer [250 mM sodium phosphate (pH 7.0), 50 mM DTT, 5 mM EDTA].

Cat. #	Product	Size	Price	License	Quantity	Details
7334	Pfu Pyroglutamate Aminopeptidase	10 mU	USD $383.00
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]. Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components Image Data Back Pfu Pyroglutamate Aminopeptidase Activity Pfu Pyroglutamate Aminopeptidase Activity. Back 7334: Pfu Pyroglutamate Aminopeptidase

More Information

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 Pyrococcus furiosus pyroglutamate aminopeptidase gene.

Properties

Systematic name:	L-Pyrrolidone carboxyl peptidase
Enzyme code:	3.4.19.3
Molecular weight:	24.072 kDA (calculated), 28 kDA (by SDS-PAGE)
Optimum temperature:	95–100°C
Thermo stability:	~90% activity at 75°C; pH 7.0, 150 min
Optimum pH:	6.0–9.0; ≥80% activity in a pH range of 5.0–9.0 at 75°C when reactivated for 30 min
Tolerance to denaturants:	≤1 M Urea, ≤1 M Guanidine-HCL, ≤0.01% SDS
Inhibitors:	PCMB, Hg²⁺

Definition of activity

One unit of enzyme activity corresponds to the amount required to hydrolyze 1 µmol pyroglutamate p-nitroanilide at 37°C in 1 minute at pH 7.0.

References

Hamazume, Y. & Mega, T. Positions of Disulfide Bonds in Riboflavin-Binding Protein of Hen Egg White. J. Biochem 101, 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).

Additional product information

Please see the product's Certificate of Analysis for information about storage conditions, product components, and technical specifications. Please see the Kit Components List to determine kit components. Certificates of Analysis and Kit Components Lists are located under the Documents tab.

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