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Merck

SAE0215

Sigma-Aldrich

Inorganic Pyrophosphatase from Escherichia coli

≥100 units/mL, buffered aqueous solution

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352204

biológiai forrás

Escherichia coli

Minőségi szint

rekombináns

expressed in E. coli

grade

for molecular biology

leírás

Recombinant, expressed in E.coli

Teszt

≥95% (size exclusion chromatography)

Forma

buffered aqueous solution

specifikus aktivitás

≥100 units/mL

eltarthatósági idő

2 yr at -20 °C ((retest))

molekulatömeg

19.7 kDa

tárolási körülmény

OK to freeze

koncentráció

≥100 units/mL

szín

colorless

optimális pH

9.0 (25 °C)

pH

8.0 (25 °C)

oldhatóság

soluble
water: miscible

alkalmasság

suitable for molecular biology

UniProt elérési szám

alkalmazás(ok)

research use

idegen aktivitás

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

kiszállítva

dry ice

tárolási hőmérséklet

-10 to -25°C

Általános leírás

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).

Alkalmazás

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.

Biokémiai/fiziológiai hatások

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.

Tulajdonságok és előnyök

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

Egység definíció

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.

Fizikai forma

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.

Tárolási osztály kódja

10 - Combustible liquids

WGK

WGK 1


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Dokumentumtár megtekintése

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
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

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