A8200
Aminopeptidase from Aeromonas proteolytica
lyophilized powder, 50-150 units/mg protein
Sinónimos:
AAP, Aminopeptidase from Vibrio proteolyticus, bacterial leucyl aminopeptidase
Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización
About This Item
Número de CAS:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Productos recomendados
grade
Proteomics Grade
Quality Level
form
lyophilized powder
specific activity
50-150 units/mg protein
mol wt
29.5 kDa
composition
Protein, ~40% biuret
solubility
H2O: soluble 0.9-1.1 mg/mL, clear, colorless
foreign activity
endopeptidase, essentially free
storage temp.
−20°C
General description
A zinc-containing enzyme.
Specificity
Catalyzes the release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
Application
Aminopeptidases are a family of widely distributed proteases, which may be used to study many significant biological processes such as protein maturation, hormone production, and peptide digestion. The enzyme has been used to measure the kinetic rate constant for the binding of bestatin, a general protease inhibitor, to aminopeptidase.
Biochem/physiol Actions
Aminopeptidase from Aeromonas proteolytica is a metalloenzyme, which contains 2 atoms of Zn2+ in a single polypeptide with an approximate molecular weight of 29.5 kDa as determined by sedimentation. This enzyme has a high degree of stability, being stable even at temperatures of 70 °C for several hours. Partial inactivation occurs in 8 M urea. Maximum stability and activity are between pH 8.0-8.5. Aminopeptidase from Aeromonas proteolytica can function as an esterase.
Aminopeptidase from Aeromonas proteolytica is involved in protein maturation, hormone production and peptide digestion.
Unit Definition
One unit will hydrolyze 1.0 μmole of L-leucine p-nitroanilide to L-leucine and p-nitroaniline per min at pH 8.0 at 25 °C.
Physical form
Lyophilized powder containing tricine buffer, pH 8.0, zinc chloride and stabilizer.
Preparation Note
Dissolves in water at 0.9-1.1 mg/mL concentration to form a clear, colorless solution.
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
ppe
Eyeshields, Gloves, type N95 (US)
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
¿Ya tiene este producto?
Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Los clientes también vieron
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
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
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
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
Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.
Póngase en contacto con el Servicio técnico