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Merck
CN

A4987

Aminopeptidase His-tagged from Vibrio proteolyticus

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关于此项目

UNSPSC Code:
12352204
EC Number:
232-874-6
NACRES:
NA.54
EC 号:
3.4.11.10
Specific activity:
50-100 U/mg
Recombinant:
expressed in E. coli
Shelf life:
2 yr
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recombinant

expressed in E. coli

Quality Level

grade

Proteomics Grade

form

powder

specific activity

50-100 U/mg

shelf life

2 yr

shipped in

wet ice

storage temp.

−20°C

Other Notes

One unit will hydrolyze 1.0 micromole of Leucine P-Nitroanilide to L-Leucine and P-Nitroaniline per minute at pH 8.0 at 25°C.

pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

存储类别

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

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分析证书(COA)

Lot/Batch Number

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C Schalk et al.
Archives of biochemistry and biophysics, 294(1), 91-97 (1992-04-01)
The heat-stable aminopeptidase from Aeromonas proteolytica has been purified using two new procedures, with the aim of preparing large single crystals for X-ray analysis. In a first procedure, we tried to avoid any drastic conditions capable of inducing microheterogeneities in
William T Desmarais et al.
Structure (London, England : 1993), 10(8), 1063-1072 (2002-08-15)
The aminopeptidase from Aeromonas proteolytica (AAP) is a bridged bimetallic enzyme that removes the N-terminal amino acid from a peptide chain. To fully understand the metal roles in the reaction pathway of AAP we have solved the 1.20 A resolution
Mariam Hartley et al.
Protein expression and purification, 66(1), 91-101 (2009-02-24)
Metalloaminopeptidases (mAPs) are enzymes that are involved in HIV infectivity, tumor growth and metastasis, angiogenesis, and bacterial infection. Investigation of structure-function relationships in mAPs is a prerequisite to rational design of anti-mAP chemotherapeutics. The most intensively studied member of the
D Mahadevan et al.
Protein science : a publication of the Protein Society, 8(11), 2546-2549 (1999-12-14)
The Aeromonas proteolytica aminopeptidase (AMP), Pseudomonas sp. (RS-16) carboxypeptidase G2 (CPG2), and Streptomyces griseus aminopeptidase (SGAP) are zinc dependent proteolytic enzymes with cocatalytic zinc ion centers and a conserved aminopeptidase fold. A BLAST search with the sequence of the solved
Krzysztof P Bzymek et al.
The Journal of biological chemistry, 279(30), 31018-31025 (2004-05-13)
Glutamate 151 has been proposed to act as the general acid/base during the peptide hydrolysis reaction catalyzed by the co-catalytic metallohydrolase from Aeromonas proteolytica (AAP). However, to date, no direct evidence has been reported for the role of Glu-151 during

全球贸易项目编号

货号GTIN
A4987-100UN04061832699554
A4987-250UN04061832699561

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