P6236
Pyroglutamate Aminopeptidase from Pyrococcus furiosus
recombinant, expressed in E. coli, ~90% (SDS-PAGE), ≥5.0 units/mg protein
Sinónimos:
L-Pyrrolidone carboxyl peptidase
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About This Item
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
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Productos recomendados
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
Categorías relacionadas
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.[1]
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.[2]
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.[3] The levels PGP 1 is elevated during inflammation.[4]
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.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Los clientes también vieron
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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