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Merck

P6236

Pyroglutamate Aminopeptidase from Pyrococcus furiosus

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

Synonim(y):

L-Pyrrolidone carboxyl peptidase

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Informacje o tej pozycji

UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-981-8
MDL number:
Specific activity:
≥5.0 units/mg protein
Assay:
~90% (SDS-PAGE)
Recombinant:
expressed in E. coli

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recombinant

expressed in E. coli

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

Quality Level

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Ta pozycja
M6435A9934A8200
assay

~90% (SDS-PAGE)

assay

≥93% (SDS-PAGE)

assay

-

assay

-

specific activity

≥5.0 units/mg protein

specific activity

0.5 units/mg protein

specific activity

≥200 units/mg protein

specific activity

50-150 units/mg protein

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

-

recombinant

-

form

lyophilized powder

form

solution

form

lyophilized powder

form

lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

mol wt

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

mol wt

37 kDa by SDS-PAGE

mol wt

21 kDa by gel filtration, 33 kDa by SDS-PAGE

mol wt

29.5 kDa

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

Thermostable aminopeptidase that liberates N-terminal pyroglutamic acid from proteins and peptides prior to Edman degradation.
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.[1]
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.

Biochem/physiol Actions

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.
Pyroglutamate Aminopeptidase (PGP 1) interacts with immunoglobulin, functions as inflammatory cytokine and modulates immune response. The levels PGP 1 is elevated during inflammation.

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.

Other Notes

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

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Klasa składowania

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

New deblocking aminopeptidases from Pyrococcus horikoshii
Mori K and Ishikawa K
Bioscience, Biotechnology, and Biochemistry, 69(10), 1854-1860 (2005)
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
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)
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)
William E Werner et al.
Analytical biochemistry, 342(1), 120-125 (2005-06-17)
Typically, the removal of pyroglutamate from the protein chains of immunoglobulins with the enzyme pyroglutamate aminopeptidase requires the use of chaotropic and reducing agents, quite often with limited success. This article describes a series of optimization experiments using elevated temperatures

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