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P6236

Sigma-Aldrich

Pyroglutamate Aminopeptidase from Pyrococcus furiosus

recombinant, expressed in E. coli, ~90% (SDS-PAGE), ≥5.0 units/mg protein

Synonym(s):

L-Pyrrolidone carboxyl peptidase

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About This Item

Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

Assay

~90% (SDS-PAGE)

form

lyophilized powder

specific activity

≥5.0 units/mg protein

mol wt

24.072 kDa by amino acid sequence
28 kDa by SDS-PAGE

shipped in

dry ice

storage temp.

−20°C

Related Categories

General description

Pyroglutamate Aminopeptidase from Pyrococcus furiosus, also called the deblocking aminopeptidase, is a 42 kDa protein and belongs to aminopeptidase A family. It shares sequence homology with aminopeptidase in the active site, with conserved zinc and cobalt binding residues.

Application

Pyroglutamate Aminopeptidase, from Pyrococcus furiosus is a recombinant, thermostable aminopeptidase that is expressed in Escherichia coli. It is used to cleave pyroglutamic acid which allows analysis of N-terminal sequences of peptides.
The enzyme from Sigma has been used for the removal of pyroglutamate (pGlu) N-terminal blocking group, under reduced conditions, prior to N-terminal sequencing of purified cassiicolin.
Thermostable aminopeptidase that liberates N-terminal pyroglutamic acid from proteins and peptides prior to Edman degradation.

Biochem/physiol Actions

Pyroglutamate Aminopeptidase (PGP 1) interacts with immunoglobulin, functions as inflammatory cytokine and modulates immune response. The levels PGP 1 is elevated during inflammation.
This enzyme is specific for N-terminal pyroglutamic acids. It cleaves the N-terminal pyroglutamic acid from proteins and peptides prior to Edman degradation. The optimal temperature range is 95 to 100 °C and the optimal pH range is 6.0 to 9.0.

Unit Definition

One unit will hydrolyze 1 μmol of pyroglutamate p-nitroanilide per minute at pH 7.0 at 37 °C.

Physical form

Lyophilized powder containing sodium phosphate

Preparation Note

Reconstitute the vial of enzyme with 50 μl of 50 mM sodium phosphate, pH 7.0, with 10 mM DTT and 1 mM EDTA. The reconstituted solution should be stored at -20 °C.

Pictograms

Health hazardExclamation mark

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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New deblocking aminopeptidases from Pyrococcus horikoshii
Mori K and Ishikawa K
Bioscience, Biotechnology, and Biochemistry, 69(10), 1854-1860 (2005)
A Ultrasensitive Near-Infrared Fluorescent Probe Reveals Pyroglutamate Aminopeptidase 1 Can Be a New Inflammatory Cytokine
Gong Q, et al.
Advanced science (Weinheim, Baden-Wurttemberg, Germany), 5(4), 1700664-1700664 (2018)
Pyroglutamate aminopeptidase 1 may be an indicator of cellular inflammatory response as revealed using a sensitive long-wavelength fluorescent probe
Gong Q, et al.
Chemical Science, 7(7), 4694-4697 (2016)
Frédéric de Lamotte et al.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 849(1-2), 357-362 (2006-11-23)
Cassiicolin, a phytotoxin produced by the necrotrophic fungus Corynespora cassiicola, was purified to homogeneity from a rubber tree isolate. The optimized protocol involves reverse phase chromatography followed by size exclusion chromatography, with monitoring of the toxicity on detached rubber tree
Jai K Kaushik et al.
Biochemistry, 45(23), 7100-7112 (2006-06-07)
Pyrrolidone carboxyl peptidases (PCPs) from hyperthermophiles have a structurally conserved and completely buried Glu192 in the hydrophobic core; in contrast, the corresponding residue in the mesophile protein is a hydrophobic residue, Ile. Does the buried ionizable residue contribute to stabilization

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