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SAE0215

Inorganic Pyrophosphatase from Escherichia coli

≥100 units/mL, buffered aqueous solution

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.28
Specific activity:
≥100 units/mL
Assay:
≥95% (size exclusion chromatography)
Biological source:
Escherichia coli
Recombinant:
expressed in E. coli
Concentration:
≥100 units/mL
Shelf life:
2 yr at -20 °C ((retest))

Key Documents

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biological source

Escherichia coli

recombinant

expressed in E. coli

grade

Molecular Biology

description

Recombinant, expressed in E.coli

assay

≥95% (size exclusion chromatography)

form

buffered aqueous solution

specific activity

≥100 units/mL

shelf life

2 yr at -20 °C ((retest))

mol wt

19.7 kDa

storage condition

OK to freeze

concentration

≥100 units/mL

color

colorless

optimum pH

9.0 (25 °C)

pH

8.0 (25 °C)

solubility

soluble, water: miscible

suitability

suitable for molecular biology

UniProt accession no.

P0A7A9

application(s)

research use

foreign activity

DNAse, none detected
RNAse, none detected
Nickase, none detected

shipped in

dry ice

storage temp.

-10 to -25°C

Quality Level

200

General description

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).

Application

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.

Biochem/physiol Actions

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.

Features and Benefits

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

Physical form

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.

Other Notes

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.

Storage Class

10 - Combustible liquids

wgk

WGK 1

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
0000336817
0000336816
0000322675
0000336817
0000336816

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Andrew C Pratt et al.
Journal of structural biology, 192(1), 76-87 (2015-08-25)
Family I inorganic pyrophosphatases (PPiases) are ubiquitous enzymes that are critical for phosphate metabolism in all domains of life. The detailed catalytic mechanism of these enzymes, including the identity of the general base, is not fully understood. We determined a
R Lahti et al.
Journal of bacteriology, 170(12), 5901-5907 (1988-12-01)
Escherichia coli K-12 gene ppa encoding inorganic pyrophosphatase (PPase) was cloned and sequenced. The 5' end of the ppa mRNA was identified by primer extension mapping. A typical E. coli sigma 70 promoter was identified immediately upstream of the mRNA
B S Cooperman et al.
Trends in biochemical sciences, 17(7), 262-266 (1992-07-01)
Soluble inorganic pyrophosphatases (PPases) are essential enzymes that are important for controlling the cellular levels of inorganic pyrophosphate (PPi). Although prokaryotic and eukaryotic PPases differ substantially in amino acid sequence, recent evidence now demonstrates clearly that PPases throughout evolution show
A A Baykov et al.
Biochemistry, 35(15), 4655-4661 (1996-04-16)
Steady-state rates of PPi hydrolysis by Escherichia coli inorganic pyrophosphatase (E-PPase) were measured as a function of magnesium pyrophosphatase (substrate) and free Mg2+ ion (activator) in the pH range 6.0-10.0. Computer fitting of hydrolysis data in combination with direct measures
Kyung Min Ko et al.
FEBS letters, 581(28), 5445-5453 (2007-11-06)
Inorganic pyrophosphatase (PPase) catalyzes the hydrolysis of inorganic pyrophosphate (PPi) into phosphate (Pi), which provides a thermodynamic driving force for important biosynthetic reactions. The nematode Caenorhabditis elegans gene C47E12.4 encodes a PPase (PYP-1) which shows 54% amino acid identity with
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