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Merck
CN

19924

Pyroglutamate Aminopeptidase from Pyrococcus furiosus, recombinant from E. coli

7-13 mU (per vial)

Synonym(s):

Pyrase, Pyroglutamyl-Peptidase I, Pyrrolidone Carboxyl Peptidase

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About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-981-8
MDL number:
EC Number:
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Product Name

Pyroglutamate Aminopeptidase from Pyrococcus furiosus, recombinant from E. coli, 7-13 mU (per vial)

recombinant

expressed in E. coli

form

lyophilized

specific activity

7-13 mU (per vial)

mol wt

Mr ~28000

storage temp.

−20°C

Analysis Note

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+.

Other Notes

1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol Pyroglutamate-p-nitroanilide per minute at pH 7.0 and 37 °C
An enzyme that removes pyroglutamic acid (pGlu) from pGlu-peptide and proteins; employed in Edman degradation.

Packaging

package of 0.01 Unit

pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

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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
Naiara Agirregoitia et al.
Regulatory peptides, 139(1-3), 52-58 (2006-11-25)
Prolyl endopeptidase and pyroglutamyl peptidase I are enzymes which participate in the degradation of thyrotropin-releasing hormone (TRH), a hormone which is thought to play an important role in the development of organs and tissues. Here, we have characterized the ontogeny
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
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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