Inorganic Pyrophosphatase from Escherichia coli

Inorganic pyrophosphatase (PPase) is a ubiquitous enzyme that catalyzes pyrophosphate hydrolysis. It plays an important role in energy metabolism by providing a thermodynamic pull for biosynthetic reactions, such as protein, RNA, and DNA synthesis. Nucleic acid synthesis would be energetically impossible in vivo if not coupled with the hydrolysis of pyrophosphate (PPi).

This product is based on the native pyrophosphatase from E. coli, Uniprot No. P0A7A9. Pyrophosphatase in E. coli is a homohexameric protein containing 175 amino acids residues per subunit. This product is a recombinant protein expressed in E. coli and induced by IPTG. Each subunit has a MW of 19.7 kDa and theoretical pI of ~5. The protein activity is Mg2+ dependent and it is a relatively thermostable protein.

Inorganic pyrophosphatase (PPase) is a ubiquitous enzyme that catalyzes pyrophosphate to phosphate. It plays an important role in energy metabolism as it provides a thermodynamic pull for biosynthetic reactions, such as protein, RNA, and DNA synthesis.

This product has a purity minimum of 95% (SEC-HPLC) and an activity minimum of 100 units/mL to enhance RNA yield during transcription.

The product is supplied as an aqueous solution containing 20mM Tris-HCl, 100mM NaCl, 1mM DTT, 0.1mM EDTA, and 50% glycerol, titrated to pH 8 at 25 °C.

One unit will release 1.0 µmole of inorganic orthophosphate per minute at pH 9 at 25 °C. The reaction buffer used for determination of enzyme activity contains 50 mM Tris-HCl, pH 9.0.