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Key Documents

I5907

Sigma-Aldrich

Pyrophosphatase, Inorganic from Escherichia coli

recombinant, expressed in E. coli, lyophilized powder, ≥90%, ≥800 units/mg protein

Synonyma:

Inorganic Pyrophosphatase, Pyrophosphate phosphohydrolase

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen


About This Item

Číslo CAS:
Číslo enzymu podle klasifikace EK:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

assay

≥90%

form

lyophilized powder

specific activity

≥800 units/mg protein

mol wt

hexamer subunit mol wt 20 kDa

storage temp.

−20°C

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General description

Pyrophosphatase from E coli (E-PPase) has a broader pH optimum and contains four divalent cations per subunit. It comprises 175 amino acids with additional aspartate residue in the active site cavity. Structurally E-PPase is a homohexamer with six identical 20 kDa subunits. Magnesium is a cofactor for E-PPase.

Application

Inorganic pyrophosphatase (PPase) is a ubiquitous enzyme catalyzing the reaction PPi + H2O → 2Pi.
It plays an important role in protein, RNA, and DNA synthesis.
Pyrophosphatase, Inorganic from Escherichia coli has been used as a component of transcription buffer.
Pyrophosphatase, inorganic from Escherichia coli has been used in assay for conjugation of ubiquitin and ubiquitin-like proteins. It has been used for one-pot three-enzyme system for synthesis of Lewis x and sialyl Lewis x antigens.

Biochem/physiol Actions

Pyrophosphatase from E coli (E-PPase) is an essential enzyme in yeast and bacteria The active site residues are crucial for binding to magnesium.

Other Notes

A homohexameric protein containing 175 amino acid residues per subunit, its activity is Mg2+ dependent. It is a relatively thermostable protein.

Unit Definition

One unit will release 1.0 μmole of inorganic orthophosphate per minute at pH 9 at 25 °C.

Physical form

Lyophilized powder in Tris-buffered salts containing protease inhibitors

pictograms

Exclamation mark

signalword

Warning

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Zákazníci si také prohlíželi

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The structure of E. coli soluble inorganic pyrophosphatase at 2.7
Kankare J, et al.
Protein engineering, design & selection : PEDS, 7(7), 823-830 (1994)
Christopher E Berndsen et al.
Analytical biochemistry, 418(1), 102-110 (2011-07-21)
Ubiquitination is a widely studied regulatory modification involved in protein degradation, DNA damage repair, and the immune response. Ubiquitin is conjugated to a substrate lysine in an enzymatic cascade involving an E1 ubiquitin-activating enzyme, an E2 ubiquitin-conjugating enzyme, and an
Ngoc Truongvan et al.
Nature communications, 13(1), 4789-4789 (2022-08-16)
The covalent modification of target proteins with ubiquitin or ubiquitin-like modifiers is initiated by E1 activating enzymes, which typically transfer a single modifier onto cognate conjugating enzymes. UBA6 is an unusual E1 since it activates two highly distinct modifiers, ubiquitin
Directed evolution of glycopeptides using mRNA display
Horiya S, et al.
Methods in Enzymology, 597, 83-141 (2017)
Structure and function analysis of Escherichia coli inorganic pyrophosphatase: is a hydroxide ion the key to catalysis?
Salminen, T, et al.
Biochemistry, 34(3), 782-791 (1995)

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