A4987
Aminopeptidase His-tagged from Vibrio proteolyticus
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About This Item
Recommended Products
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.
signalword
Danger
hcodes
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
Certificates of Analysis (COA)
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Gudrun Schürer et al.
Biochemistry, 43(18), 5414-5427 (2004-05-05)
The aminopeptidase of Aeromonas proteolytica (AAP) belongs to the group of metallo-hydrolases that require two divalent cations for full activity. Such binuclear metal centers are found in several aminopeptidases, raising the question whether a common mechanism, at least partly, is
G Van Heeke et al.
Biochimica et biophysica acta, 1131(3), 337-340 (1992-07-15)
The gene encoding the Vibrio proteolyticus aminopeptidase was cloned and sequenced and its amino acid sequence was deduced. The gene encodes a 54 kDa protein, larger than the previously reported size of 30 kDa for the purified aminopeptidase. Sequence alignments
L Ustynyuk et al.
Biochemistry, 38(35), 11433-11439 (1999-09-02)
Seven aliphatic and two aromatic alcohols were tested as reporters of the substrate selectivity of the aminopeptidase from Aeromonas proteolytica (AAP). This series of alcohols was chosen to systematically probe the effect of carbon chain length, steric bulk, and inhibitor
Carin C Stamper et al.
Biochemistry, 43(30), 9620-9628 (2004-07-28)
Binding of the competitive, slow-binding inhibitor bestatin ([(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoy]-leucine) to the aminopeptidase from Aeromonas proteolytica (AAP) was examined by both spectroscopic and crystallographic methods. Electronic absorption spectra of the catalytically competent [Co_(AAP)], [CoCo(AAP)], and [ZnCo(AAP)] enzymes recorded in the presence of
Krzysztof P Bzymek et al.
Inorganic chemistry, 44(23), 8574-8580 (2005-11-08)
Previous kinetic characterization of the glutamate 151 (E151)-substituted forms of the leucine aminopeptidase from Aeromonas proteolytica (Vibrio proteolyticus; AAP) has provided critical evidence that this residue functions as the general acid/base. The close proximity of similar glutamate residues to the
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