Pfu Methionine Aminopeptidase
Pfu Methionine Aminopeptidase
Brand: Takara Bio.
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Pfu Methionine Aminopeptidase
Pfu Methionine Aminopeptidase is a thermostable Methionine Aminopeptidase isolated from Pyrococcus furiosus and produced as a recombinant protein. This enzyme liberates the N-terminal methionine residue from proteins and peptides.
Applications
- Release of N-terminal methionine residues from recombinant proteins and peptides
Source
Escherichia coli transformed with Pyrococcus furiosus methionine aminopeptidase gene.
Purity
≥95% via SDS-PAGE. No other proteases detected.
Storage
–20°C
Properties
- Molecular weight: 32.848 (MS analysis), 37.000 (SDS-PAGE)
- Optimum temperature: 85–95°C
- Thermostability: Stable for 1 hr at 75°C, pH 7.2 and 0.5 mM Co2+
- Optimum pH: 7.0–8.0
- Tolerance to denaturants: ≤2 M Urea, ≤0.2 M Guanidine-HCl, ≤0.01% SDS
- Activator: Co2+
- Inhibitor: EDTA
Form
Solution of 10 mM Tris-HCl, pH 7.5, containing 0.01% Tween 20 and 0.1 mM CoCl2
Ben-Bassat, A. et al. Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure. J. Bacteriol. 169, 751–757 (1987).
Ben-Bassat, A. et al. Amino-terminal processing of proteins. Nature 326, 315 (1987).
Miller, C.G. et al. N-terminal methionine-specific peptidase in Salmonella typhimurium. Proc. Natl. Acad. Sci. USA 84, 2718–2722 (1987).
Yasueda, H. et al. High-level direct expression of semi-synthetic human interleukin-6 in Escherichia coli and production of N-terminus met-free product. Biotechnology 8, 1036–1040 (1990).
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