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I5907

Pyrophosphatase, Inorganic from Escherichia coli

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

Synonim(y):

Inorganic Pyrophosphatase, Pyrophosphate phosphohydrolase

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1 MG

1760,00 zł

1760,00 zł

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Informacje o tej pozycji

Numer CAS:
9024-82-2
UNSPSC Code:
12352204
NACRES:
NA.32
EC Number:
232-784-7
MDL number:
MFCD00131379
Numer WE:
3.6.1.1 (BRENDA, IUBMB)
Specific activity:
≥800 units/mg protein
Assay:
≥90%
Recombinant:
expressed in E. coli

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recombinant

expressed in E. coli

Quality Level

200

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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Ta pozycja
P5931I1643F3174
Pyrophosphatase, Inorganic from Escherichia coli recombinant, expressed in E. coli, lyophilized powder, ≥90%, ≥800 units/mg protein

Sigma-Aldrich

I5907

Pyrophosphatase, Inorganic from Escherichia coli

Phosphatase, Alkaline from Escherichia coli lyophilized powder, 30-60 units/mg protein (in glycine buffer)

Sigma-Aldrich

P5931

Phosphatase, Alkaline from Escherichia coli

Pyrophosphatase, Inorganic from baker’s yeast (S. cerevisiae) powder, ≥500 units/mg protein (E1%/280)

Sigma-Aldrich

I1643

Pyrophosphatase, Inorganic from baker′s yeast (S. cerevisiae)

Fpg Protein from Escherichia coli ≥90% (SDS-PAGE), buffered aqueous glycerol solution, >20,000 units/mg protein, suitable for genomic analysis

Sigma-Aldrich

F3174

Fpg Protein from Escherichia coli

assay

≥90%

assay

-

assay

-

assay

≥90% (SDS-PAGE)

specific activity

≥800 units/mg protein

specific activity

30-60 units/mg protein (in glycine buffer)

specific activity

≥500 units/mg protein (E1%/280)

specific activity

>20,000 units/mg protein

form

lyophilized powder

form

lyophilized powder

form

powder

form

buffered aqueous glycerol solution

recombinant

expressed in E. coli

recombinant

-

recombinant

-

recombinant

expressed in E. coli

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

mol wt

hexamer subunit mol wt 20 kDa

mol wt

-

mol wt

71 kDa

mol wt

30.2 kDa (269 amino acids, predicted from the nucleotide sequence)

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.[1]

Application

Pyrophosphatase, Inorganic from Escherichia coli has been used as a component of transcription buffer.
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 in assay for conjugation of ubiquitin and ubiquitin-like proteins.[2] It has been used for one-pot three-enzyme system for synthesis of Lewis x and sialyl Lewis x antigens.[3]

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.

Physical form

Lyophilized powder in Tris-buffered salts containing protease inhibitors

Other Notes

A homohexameric protein containing 175 amino acid residues per subunit, its activity is Mg2+ dependent. It is a relatively thermostable protein.
One unit will release 1.0 μmole of inorganic orthophosphate per minute at pH 9 at 25 °C.
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pictograms

Exclamation mark
GHS07

signalword

Warning

Hazard Classifications

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

target_organs

Respiratory system

Klasa składowania

11 - Combustible Solids

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certyfikaty analizy (CoA)

Lot/Batch Number
0000476640
0000476640
0000365108
0000173793
0000365108

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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
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
Hai Yu et al.
Current protocols in chemical biology, 4, 233-247 (2012-09-01)
L-Fucose has been found abundantly in human milk oligosaccharides, bacterial lipopolysaccharides, glycolipids, and many
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)
Elodie Laine et al.
Proceedings of the National Academy of Sciences of the United States of America, 107(25), 11277-11282 (2010-06-11)
Allostery plays a key role in the regulation of the activity and function of many biomolecules. And although many ligands act through allostery, no systematic use is made of it in drug design strategies. Here we describe a procedure for
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SKUNUMER GTIN
I5907-1MG04061833857649

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