- Liberation of N-terminal formyl, acetyl and myristyl blocking groups from proteins
|Volume: ||1 mL|
|Components: ||250 mM N-Ethylmorpholine-AcOH buffer|
| ||(pH 8.0, 0.5 mM CoCl2)|
|Once thawed, the buffer should be stored at 4°C. Avoid additional freeze-thaw cycles.|
Recombinant yeast containing the gene encoding Pyrococcus furiosus Ac-DAP.
Homogeneous on PAGE
–20°C. Once thawed, the enzyme solution should be stored at 4°C. The thawed enzyme and buffer are stable for at least 3 months at 4°C.
This enzyme cannot react with proteins containing higher order structures; protein samples should be denatured by chemical procedures such as carboxymethylation. This enzyme cannot react with proteins blotted onto PVDF membranes.
- Specific activity: >8 units/mg
- Protein concentration: 1 mg/mL
- Molecular weight: 38,639 Da (mass spectrometry), ~451 kDa (sedimentation equilibrium method)
- Activator: CoCl2
- Inhibitor: Amastatin, EDTA
- Optimum pH: 6.5–9.0
- Optimum Temperature: 85–95°C
- Thermal Stability: Enzyme retains 100% activity after 48 hrs. at 50°C in the supplied buffer (pH 8.0, 0.1 mM Co2+)
- N-terminal amino acid sequence: Ac-MDDYELLKKVVEADGV...
In a solution of 50 mM N-Ethylmorpholine-AcOH buffer (pH 8.0)
Definition of Activity
One unit of activity corresponds to the amount of enzyme required to hydrolyze 1 µmol of leucine-p-nitroanilide at 75°C and pH 8.0 in one minute.