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Merck

SAE0215

Sigma-Aldrich

Inorganic Pyrophosphatase from Escherichia coli

≥100 units/mL, buffered aqueous solution

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About This Item

Código UNSPSC:
12352204

origen biológico

Escherichia coli

Nivel de calidad

recombinante

expressed in E. coli

grado

for molecular biology

descripción

Recombinant, expressed in E.coli

Ensayo

≥95% (size exclusion chromatography)

Formulario

buffered aqueous solution

actividad específica

≥100 units/mL

caducidad

2 yr at -20 °C ((retest))

mol peso

19.7 kDa

condiciones de almacenamiento

OK to freeze

concentración

≥100 units/mL

color

colorless

pH óptimo

9.0 (25 °C)

pH

8.0 (25 °C)

solubilidad

soluble
water: miscible

idoneidad

suitable for molecular biology

Nº de acceso UniProt

aplicaciones

research use

actividad extraña

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

Condiciones de envío

dry ice

temp. de almacenamiento

-10 to -25°C

Descripción general

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).

Aplicación

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.

Acciones bioquímicas o fisiológicas

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.

Características y beneficios

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

Definición de unidad

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.

Forma física

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.

Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 1


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A Salminen et al.
The Journal of biological chemistry, 274(48), 33898-33904 (1999-11-24)
A homohexameric molecule of Escherichia coli pyrophosphatase is arranged as a dimer of trimers, with an active site present in each of its six monomers. Earlier we reported that substitution of His(136) and His(140) in the intertrimeric subunit interface splits
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
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

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