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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

Synonyme(s) :

Inorganic Pyrophosphatase, Pyrophosphate phosphohydrolase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32

Produit recombinant

expressed in E. coli

Niveau de qualité

Pureté

≥90%

Forme

lyophilized powder

Activité spécifique

≥800 units/mg protein

Poids mol.

hexamer subunit mol wt 20 kDa

Température de stockage

−20°C

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Description générale

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.

Actions biochimiques/physiologiques

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

Autres remarques

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

Définition de l'unité

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

Forme physique

Lyophilized powder in Tris-buffered salts containing protease inhibitors

Pictogrammes

Exclamation mark

Mention d'avertissement

Warning

Mentions de danger

Classification des risques

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

Organes cibles

Respiratory system

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Les clients ont également consulté

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
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)
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Current protocols in chemical biology, 4, 233-247 (2012-09-01)
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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
Rahul Sadavarte et al.
Biotechnology progress, 33(1), 133-139 (2016-11-01)
Heterologous overexpression of genes in Escherichia coli has made it possible to obtain high titers of recombinant proteins. However, this can result in the formation of aggregated protein particles known as 'inclusion bodies'. Protein sequestered as inclusion body is inactive

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