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Aminopeptidase from Aeromonas proteolytica

SIGMA/A8200 - lyophilized powder, 50-150 units/mg protein

Synonym: AAP; Aminopeptidase from Vibrio proteolyticus; bacterial leucyl aminopeptidase

CAS Number: 37288-67-8
EC Number: 232-874-6
MDL Number: MFCD00166325
Product Type: Chemical

Catalog Number PKG Qty. Price Quantity
45-A8200-100UN 100 units
$483.00
1/EA
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45-A8200-250UN 250 units
$960.00
1/EA
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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.
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: A8200-100UN
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: A8200-250UN

 

composition Protein, ~40% biuret
foreign activity endopeptidase, essentially free
form lyophilized powder
grade Proteomics Grade
mol wt 29.5 kDa
Quality Level 300 
solubility H2O: soluble 0.9-1.1 mg/mL, clear, colorless
specific activity 50-150 units/mg protein
storage temp. −20°C
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.
Biochem/physiol Actions: Aminopeptidase from Aeromonas proteolytica is involved in protein maturation, hormone production and peptide digestion.
Biochem/physiol Actions: Catalyzes the release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
General description: A zinc-containing enzyme.
Other Notes: 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.
Packaging: 100, 250 units in glass bottle
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.
activity specific activity: 50-150 units/mg protein
Storage Temp. −20°C
Enzyme Commission (EC) Number 3.4.11.10   ( BRENDA  | IUBMB  )
UNSPSC 12352204

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