Skip to Content
Merck
CN
All Photos(2)

Documents

Safety Information

A4987

Sigma-Aldrich

Aminopeptidase His-tagged from Vibrio proteolyticus

Sign Into View Organizational & Contract Pricing


About This Item

Enzyme Commission number:
3.4.11.10
EC Number:
UNSPSC Code:
12352204
NACRES:
NA.54

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

Related Categories

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

Signal Word

Danger

Hazard Statements

Hazard Classifications

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

Target Organs

Respiratory system

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

新产品

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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
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
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
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
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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service