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19924

Sigma-Aldrich

Pyroglutamataminopeptidase aus Pyrococcus furiosus, rekombinant aus E. coli

7-13 mU (per vial)

Synonym(e):

Pyrase, Pyroglutamyl-Peptidase I, Pyrrolidon-Carboxyl-Peptidase

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About This Item

CAS-Nummer:
9075-21-2
EC-Nummer:
3.4.19.3 (BRENDA, IUBMB)
EG-Nummer:
232-981-8
MDL-Nummer:
MFCD00132139
UNSPSC-Code:
12352204
NACRES:
NA.54

Rekombinant

expressed in E. coli

Qualitätsniveau

100

Form

lyophilized

Spezifische Aktivität

7-13 mU (per vial)

Mol-Gew.

Mr ~28000

Lagertemp.

−20°C

Verwandte Kategorien

Verpackung

Packung mit 0.01 Unit

Einheitendefinition

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

Hinweis zur Analyse

Enzym Aktivität: die opimale Temperatur ist 95-100° (stabil bis zu 75°C), der optimale pH ist 6-9 (stabil von pH 6-9); Inhibitoren: PCMB, Hg+

Sonstige Hinweise

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

Piktogramme

Health hazardExclamation mark
GHS08,GHS07

Signalwort

Danger

Gefahreneinstufungen

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

Zielorgane

Respiratory system

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Analysenzertifikate (COA)

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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
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
Marie Schaeffer et al.
Molecular and biochemical parasitology, 150(2), 318-329 (2006-10-10)
Pyroglutamyl peptidases I (PPI) are cysteine peptidases of the clan CF, family C15, which hydrolyse N-terminal l-pyroglutamyl residues (l-pGlu). The l-pGlu modification is a post-transcriptional modification that confers relative aminopeptidase resistance and, in some cases, is essential to the modified
Johanna L Hellström et al.
Biochimica et biophysica acta, 1764(11), 1735-1740 (2006-10-20)
To enable Edman sequencing of pyroglutamylated immunoglobulins, enzymatic deblocking by pyroglutamate aminopeptidase is performed, often with variable yield and compromised solubility. Recently, enzymatic deblocking of immunoglobulins without denaturation was described. Although the conditions ensured efficient removal of pyroglutamyl residues, we
Noriko Higaki-Sato et al.
Journal of agricultural and food chemistry, 54(19), 6984-6988 (2006-09-14)
In order to determine pyroglutamic acid levels in plasma, we developed a method based on precolumn derivatization of the carboxyl group of pyroglutamic acid with 2-nitrophenylhydrazine. Eight-week-old male SD strain rats were administered 200 mg of an acidic peptide fraction
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