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Merck

19924

Sigma-Aldrich

Pyroglutamate Aminopeptidase from Pyrococcus furiosus, recombinant from E. coli

7-13 mU (per vial)

Sinónimos:

Pyrase, Pyroglutamyl-Peptidase I, Pyrrolidone Carboxyl Peptidase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
Número CE:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

recombinante

expressed in E. coli

formulario

lyophilized

actividad específica

7-13 mU (per vial)

mol peso

Mr ~28000

temp. de almacenamiento

−20°C

Envase

package of 0.01 Unit

Definición de unidad

1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol Pyroglutamate-p-nitroanilide per minute at pH 7.0 and 37 °C

Nota de análisis

enzyme activity: the optimum temperature is 95-100 °C (the enzyme is stable up to 75 °C), the optimum pH is 6-9 (stable from pH 6-9). Inhibitors: PCMB, Hg+.

Otras notas

An enzyme that removes pyroglutamic acid (pGlu) from pGlu-peptide and proteins; employed in Edman degradation.

Pictogramas

Health hazardExclamation mark

Palabra de señalización

Danger

Frases de peligro

Clasificaciones de peligro

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

Órganos de actuación

Respiratory system

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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J Mozdzanowski et al.
Analytical biochemistry, 260(2), 183-187 (1998-07-11)
For larger proteins, efficient deblocking prior to Edman sequencing is especially important to obtain quality, extended sequencing data which is limited by the stepwise accumulation of background from the random acid hydrolysis of the protein. Therefore, any portion that remains
A C Awadé et al.
Proteins, 20(1), 34-51 (1994-09-01)
Pyrrolidone carboxyl peptidase (EC 3.4.11.8) is an exopeptidase commonly called PYRase, which hydrolytically removes the pGlu-proteins. pGlu also known as pyrrolidone carboxylic acid may occur naturally by an enzymatic procedure or may occur as an artifact in proteins or peptides.
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
An Staes et al.
Proteomics, 8(7), 1362-1370 (2008-03-05)
We previously described a proteome-wide, peptide-centric procedure for sorting protein N-terminal peptides and used these peptides as readouts for protease degradome and xenoproteome studies. This procedure is part of a repertoire of gel-free techniques known as COmbined FRActional DIagonal Chromatography
Y Shimada et al.
Journal of biochemistry, 106(3), 383-388 (1989-09-01)
The cDNA clone of Geotrichum candidum (Geo.) lipase was isolated from the Geo. cDNA library by colony hybridization using 32P-labeled oligonucleotides corresponding to a partial amino acid sequence of this enzyme. The nucleotide sequence of the cDNA determined by the

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