Certificate of Analysis and Data Sheet

Source:

Catalog No.
ENZ-275

Description :

Aeromonas Aminopeptidase is used in the processing of pharmaceutical proteins produces by genetic engineering as well as for physical and structural investigations and for sequence and amino-terminal determinations. This exopeptidase recognizes a specific stop sign at 磵- Pro and requires a free a-amino group in the L-configuration. It is therefore suitable for the removal of the redundant N-terminal methionine often added to engineered recombinant proteins.

Physical Appearance:

Sterile filtered liquid formulation.

Formulation:

Buffered solution containing 2-5 mg/ml in 10mM Tris-HCL, 100mM NaCl, 5然 ZnSO4, pH 8.0.

Stability:

Two years when stored at ?0蚓, 2 weeks at 4蚓.
Please avoid freeze-thaw cycles.

Unit definition:

One unit of Recombinant Aeromonas Aminopeptidase will hydrolyse 1 umole of L-leucine p-nitroanilide at 25蚓 per 1 minute.

Biological Activity:

Recombinant Aeromonas Aminopeptidase was found to have an activity of 120 Units/mg protein.

Endotoxin:

Less than 0.1 ng/ug (IEU/ug) of Aminopeptidase.

Usage:

Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Protein synonyms/aliases:

Bacterial leucyl aminopeptidase precursor (EC 3.4.11.10).

Protein Family:

Belongs to the peptidase M28A family.

Protein Domains:

Domains:
•IPR007484   Peptidase M28
•IPR007280   Peptidase, archaeal and bacterial C-terminal

Protein links:

Precursor- Protein structure and amino acid sequence:

Latest Publications:

1. Hydroxamate-induced spectral perturbations of cobalt Aeromonas aminopeptidase.
J Biol Chem 1987 Jun 25;262(18):8621-5
2. Modified activity of Aeromonas aminopeptidase: metal ion substitutions and role o f substrates.
Biochemistry 1986 Dec 2;25(24):8113-7
3. Spectral and kinetic studies of metal-substituted Aeromonas aminopeptidase: nonidentical, interacting metal-binding sites.
Biochemistry 1985 Sep 24;24(20):5350-6
4. A transition-state-analog inhibitor influences zinc-binding by Aeromonas aminopeptidase.
Biochem Biophys Res Commun 1985 Aug 15;130(3):1154-60
5. One hundred fold increased activity of Aeromonas aminopeptidase by sequential substitutions with Ni(II) or Cu(II) followed by zinc.
Biochem Biophys Res Commun 1983 Jul 29;114(2):646-52
6. ES complexes of Aeromonas aminopeptidase: direct observation by stopped-flow fluorescence.
Biochem Biophys Res Commun 1983 Mar 29;111(3):946-51

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中華民國95年06月06日更新