A4987
Aminopeptidase His-tagged from Vibrio proteolyticus
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100 UNITS
1.510,00 kr.
250 UNITS
2.840,00 kr.
1.510,00 kr.
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100 UNITS
1.510,00 kr.
250 UNITS
2.840,00 kr.
About This Item
1.510,00 kr.
Please contact Customer Service for Availability
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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
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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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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
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
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
S Nirasawa et al.
The Biochemical journal, 341 ( Pt 1), 25-31 (1999-06-23)
An aminopeptidase from Aeromonas caviae T-64 was translated as a preproprotein consisting of three domains; a signal peptide (19 amino acid residues), an N-terminal propeptide (101 residues) and a mature region (273 residues). We demonstrated that a proteinase, which was
Niloufar J Ataie et al.
Biochemistry, 47(29), 7673-7683 (2008-06-26)
The chemical properties of zinc make it an ideal metal to study the role of coordination strain in enzymatic rate enhancement. The zinc ion and the protein residues that are bound directly to the zinc ion represent a functional charge/dipole
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