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Key Documents

SAE0215

Sigma-Aldrich

Inorganic Pyrophosphatase from Escherichia coli

≥100 units/mL, buffered aqueous solution

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About This Item

Code UNSPSC :
12352204

Source biologique

Escherichia coli

Niveau de qualité

Produit recombinant

expressed in E. coli

Qualité

for molecular biology

Description

Recombinant, expressed in E.coli

Pureté

≥95% (size exclusion chromatography)

Forme

buffered aqueous solution

Activité spécifique

≥100 units/mL

Durée de conservation

2 yr at -20 °C ((retest))

Poids mol.

19.7 kDa

Conditions de stockage

OK to freeze

Concentration

≥100 units/mL

Couleur

colorless

pH optimal

9.0 (25 °C)

pH

8.0 (25 °C)

Solubilité

soluble
water: miscible

Adéquation

suitable for molecular biology

Numéro d'accès UniProt

Application(s)

research use

Activité étrangère

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

Conditions d'expédition

dry ice

Température de stockage

-10 to -25°C

Description générale

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.

Actions biochimiques/physiologiques

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.

Caractéristiques et avantages

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

Définition de l'unité

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.

Forme physique

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.

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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
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
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
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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