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Products >  Protein_Research >  Protein_Sequencing_and_Analysis >  N-Terminal_Deblocking_and_Analysis >  Pfu_Aminopeptidase_I

Pfu Aminopeptidase I

Pfu Aminopeptidase I is a thermostable exo-type aminopeptidase, isolated from Pyrococcus furiosus. It is produced as a recombinant protein, which liberates the N-terminal amino acid from proteins and peptides. This enzyme has a wide range of substrate specificity, and it does not hydrolyze peptide bonds at the alpha-amino residue side of proline (X-Pro). It is significantly activated in the presence of a Co2+ ion.

At-A-Glance Documents

Applications

  • Liberates the N-terminal amino acids up to X-Pro from proteins and peptides

Source

Escherichia coli carrying plasmids encoding the Pyrococcus furiosus aminopeptidase I gene.

Purity

Homogeneous on SDS-PAGE

Properties

Molecular weight:37.483 kDa (calculated) 36-37 kDa (SDS-PAGE)
Isoelectric point:4.6–4.65
Inhibitor:EDTA (Completely inhibited at 0.1 mM)
Optimum pH:5.5–8.0 (in the presence of 20 µM Co2+, at 90°C)
Optimum Temperature:80°C (in the presence of 20 µM Co2+, pH 6.0) 95°C (without Co2+, pH 6.0)
Thermal Stability: The enzyme retains 65% activity after 4 hrs. at 90°C (pH 8.0, without Co2+).

Definition of Activity

One unit of enzyme activity corresponds to the amount required to hydrolyze 1 µmol of Leucine-p-nitroanilide at 75°C, pH 8.0, in 1 minute.

Activities

  • Approximately 84 U/mg protein (5 mM Leucine-p-nitroanilide)
  • Approximately 344 U/mg protein (in the presence of 20 µM Co2+, 5 mM Leucine-p-nitroanilide)

Form

Lyophilized




 
 
Products
Cat. # Product Package Size Price # of Units Select
7336 Pfu Aminopeptidase I 0.5 mg $132.00
 

 



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