Skip to Content
Merck

A8200

Aminopeptidase from Aeromonas proteolytica

lyophilized powder, 50-150 units/mg protein

Synonym(s):

AAP, Aminopeptidase from Vibrio proteolyticus, bacterial leucyl aminopeptidase

Slide 1 of 3
Sign In to View Organizational & Contract Pricing

Select a Size

100 UNITS

3.670,00 kr.

250 UNITS

7.320,00 kr.

3.670,00 kr.

Please contact Customer Service for Availability

About This Item

CAS Number:
37288-67-8
EC Number:
3.4.11.10 (BRENDA, IUBMB)
EC Number:
232-874-6
MDL number:
MFCD00166325
UNSPSC Code:
12352204
NACRES:
NA.54

Key Documents

View All Documentation

Skip To

Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

grade

Proteomics Grade

Quality Level

300

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

Compare Similar Items

View Full Comparison

Show Differences

1 of 4

This Item
P6236A9934P5380
Aminopeptidase from Aeromonas proteolytica lyophilized powder, 50-150 units/mg protein

Sigma-Aldrich

A8200

Aminopeptidase from Aeromonas proteolytica

Pyroglutamate Aminopeptidase from Pyrococcus furiosus recombinant, expressed in E. coli, ~90% (SDS-PAGE), ≥5.0 units/mg protein

Sigma-Aldrich

P6236

Pyroglutamate Aminopeptidase from Pyrococcus furiosus

Aminopeptidase I from Streptomyces griseus lyophilized powder, ≥200 units/mg protein

Sigma-Aldrich

A9934

Aminopeptidase I from Streptomyces griseus

Protease from Bacillus licheniformis Type VIII, lyophilized powder, 7-15 units/mg solid

Sigma-Aldrich

P5380

Protease from Bacillus licheniformis

specific activity

50-150 units/mg protein

specific activity

≥5.0 units/mg protein

specific activity

≥200 units/mg protein

specific activity

7-15 units/mg solid

grade

Proteomics Grade

grade

-

grade

-

grade

-

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

mol wt

29.5 kDa

mol wt

24.072 kDa by amino acid sequence, 28 kDa by SDS-PAGE

mol wt

21 kDa by gel filtration, 33 kDa by SDS-PAGE

mol wt

27 kDa

solubility

H2O: soluble 0.9-1.1 mg/mL, clear, colorless

solubility

-

solubility

-

solubility

10 mM NaAc (pH 7.5) and 5 mM CaAc: soluble, clear, H2O: soluble, colorless

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

General description

A zinc-containing enzyme.

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.[1]

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.[2]
Aminopeptidase from Aeromonas proteolytica is involved in protein maturation, hormone production and peptide digestion.
Catalyzes the release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.

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.

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.

Pictograms

Health hazardExclamation mark
GHS08,GHS07

Signal Word

Danger

Hazard Statements

H315,H319,H334,H335

Precautionary Statements

P302 + P352 - P305 + P351 + P338

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

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number
0000483799
0000483799
0000463785
0000463785
0000463784

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Search for a COA

Already Own This Product?

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

Visit the Document Library

James Kahn et al.
Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology, 38(4), 238-241 (2011-05-14)
We have recently designed a biochemistry laboratory experiment for the purpose of providing students an advanced experience with enzyme kinetics and the kinetics of binding. Bestatin, a well-known and commercially available general protease inhibitor, is a slow-binding inhibitor of aminopeptidase
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
K M Huntington et al.
Biochemistry, 38(47), 15587-15596 (1999-11-26)
Peptide-derived thiols of the general structure N-mercaptoacyl-leucyl-p-nitroanilide (1a-c) were synthesized and found to be potent, slow-binding inhibitors of the aminopeptidase from Aeromonas proteolytica (AAP). The overall potencies (K(I)) of these inhibitors against AAP range from 2.5 to 57 nM exceeding
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
Brian Bennett et al.
Journal of the American Chemical Society, 124(44), 13025-13034 (2002-10-31)
The aminopeptidase from Aeromonas proteolytica (AAP) was titrated with copper, which bound sequentially at two distinct sites. Both the mono- and disubstituted forms of AAP exhibited catalytic hyperactivity relative to the native dizinc enzyme. Monosubstituted AAP exhibited an axial Cu(II)
View All Related Papers

Questions

Reviews

No rating value

Active Filters

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