Inorganic Pyrophosphatase

Inorganic Pyrophosphatase is a highly thermostable enzyme derived from extremophilic bacteria. It efficiently catalyzes the hydrolysis of inorganic pyrophosphate (PPi) into two orthophosphates (Pi), relieving the inhibitory effect of PPi accumulation during nucleic acid synthesis. It is widely used in molecular biology experiments and industrial production.

PPase is purified from an E. coli strain carrying an inorganic pyrophosphatase gene cloned from Thermococcus thermophilus.

Inorganic pyrophosphatase (PPase) catalyzes the hydrolysis of inorganic pyrophosphate to produce orthophosphate.

Applicable Scenarios:

PCR/qPCR amplification, NGS sequencing, in vitro transcription (IVT) mRNA synthesis, enzymatic industrial production, DNA/RNA-related reagent development

Product Advantages:

Excellent thermostability: retains 100% activity after treatment at 100°C for 4 hours.The enzyme has a wide range of applications, including optimization of RNA transcription - increasing RNA yield in in vitro transcription reactions; optimization of PCR reactions - increasing DNA yield; removal of PPi contaminants from reagents used for SNP genotyping using the pyrophosphate assay; promoting the synthesis of proteins, RNA, and DNA; and catalyzing reactions related to PPi + H2O → 2Pi. The enzyme is highly active and thermally stable, insensitive to temperature and can be accelerated by increasing the temperature to accelerate the kinetic reaction, and remains active after repeated freezing and thawing.

Extreme heat resistance: Extremely high thermal stability, 100°C treatment for 4 hours still retains 100% activity

Significantly increases yield: Efficient hydrolysis of PPi, inhibits inhibitors, synthesis efficiency increased by 20–50%

Reaction system purity:Adaptable to various extreme reaction environments, no nuclease

contamination interference