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A4987

Sigma-Aldrich

Aminopeptidase His-tagged from Vibrio proteolyticus

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1 ML
$184.00
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$206.00
0.5 ML
$531.00
7 ML
$568.00
1 ML
$830.00

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1 ML
$184.00
0.1 ML
$206.00
0.5 ML
$531.00
7 ML
$568.00
1 ML
$830.00

About This Item

Enzyme Commission number:
3.4.11.10
EC Number:
232-874-6
UNSPSC Code:
12352204
NACRES:
NA.54

$184.00

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recombinant

expressed in E. coli

Quality Level

200

grade

Proteomics Grade

form

powder

specific activity

50-100 U/mg

shelf life

2 yr

shipped in

wet ice

storage temp.

−20°C

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species reactivity

human

species reactivity

human

species reactivity

human

species reactivity

human

antibody form

culture supernatant

antibody form

culture supernatant

antibody form

culture supernatant

antibody form

culture supernatant

biological source

rabbit

biological source

rabbit

biological source

rabbit

biological source

rabbit

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

clone

EPR3653, monoclonal

clone

EP88, monoclonal

clone

EP3622, monoclonal

clone

EP204, monoclonal

form

buffered aqueous solution

form

buffered aqueous solution

form

buffered aqueous solution

form

buffered aqueous solution

Unit Definition

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
GHS08,GHS07

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_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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    Certificates of Analysis (COA)

    Lot/Batch Number
    0000351380
    SLBC6286V
    SLBC6286

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    K M Huntington et al.
    Biochemistry, 38(47), 15587-15596 (1999-11-26)
    Peptide-derived thiols of the general structure N-mercaptoacyl-leucyl-p-nitroanilide (1a-c) were synthesized and found to be potent, slow-binding inhibitors of the aminopeptidase from Aeromonas proteolytica (AAP). The overall potencies (K(I)) of these inhibitors against AAP range from 2.5 to 57 nM exceeding
    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
    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
    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
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