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Phosphatase from Escherichia coli, Recombinant

Cat No.
NATE-1226
Description
A phosphatase is an enzyme that removes a phosphate group from its substrate by hydrolysing phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxyl group (see dephosphorylation). This action is directly opposite to that of phosphorylases and kinases, which attach phosphate groups to their substrates by using energetic molecules like ATP. A common phosphatase in many organisms is alkaline phosphatase. Another large group of proteins present in archaea, bacteria, and eukaryote exhibits deoxyribonucleotide and ribonucleotide phosphatase or pyrophosphatase activities that catalyse the decomposition of dNTP/NTP into dNDP/NDP and a free phosphate ion or dNMP/NMP and a free pyrophosphate ion. The other group of phosphatase is collectively called as protein phosphatase, which removes a phosphate group from the phosphorylated amino acid residue of the substrate protein. Protein phosphorylation is a common posttranslational modification of protein catalyzed by protein kinases, and protein phosphatases reverse the effect.
Abbr
Phosphatase, Recombinant (E. coli)
Source
Escherichia coli str. K-12 substr. MG1655
Form
Supplied in 3.2 M ammonium sulphate
Enzyme Commission Number
EC 3.1.3.-
Activity
1.905 U/mg
Molecular Weight
26827.7 Da
Purity
>95 % as judged by SDS-PAGE
Concentration
13.54 U/ml
Unit Definition
One unit is defined as the amount of enzyme required to release 1μmol of pNP per minute from pNP-phosphate (16.9 mM) in 42.4 mM sodium acetate buffer, pH 5.0, containing 6.8 mM MgCl2, at 40°C, and using an extinction coefficient of 18000 M-1cm-1.
Optimum pH
5
Optimum temperature
> 40°C
Storage
Store at 4°C (shipped at room temperature)
Preparation Instructions
Agitate vial sufficiently to fully homogenise enzyme precipitate before use.
Synonyms
HAD2
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