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SAE0215

Inorganic Pyrophosphatase from Escherichia coli

≥100 units/mL, buffered aqueous solution

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UNSPSC Code:
12352204
NACRES:
NA.28
Specific activity:
≥100 units/mL
Assay:
≥95% (size exclusion chromatography)
Biological source:
Escherichia coli
Recombinant:
expressed in E. coli
Concentration:
≥100 units/mL
Shelf life:
2 yr at -20 °C ((retest))
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biological source

Escherichia coli

Quality Segment

recombinant

expressed in E. coli

grade

Molecular Biology

description

Recombinant, expressed in E.coli

assay

≥95% (size exclusion chromatography)

form

buffered aqueous solution

specific activity

≥100 units/mL

shelf life

2 yr at -20 °C ((retest))

mol wt

19.7 kDa

storage condition

OK to freeze

concentration

≥100 units/mL

color

colorless

optimum pH

9.0 (25 °C)

pH

8.0 (25 °C)

solubility

soluble, water: miscible

suitability

suitable for molecular biology

UniProt accession no.

application(s)

research use

foreign activity

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

shipped in

dry ice

storage temp.

-10 to -25°C

General description

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.

Biochem/physiol Actions

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.

Features and Benefits

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

Physical form

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.

Other Notes

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.

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I5907P4069P5931
description

≥100 units/mL, buffered aqueous solution

description

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

description

buffered aqueous glycerol solution, 20-50 units/mg protein (in glycine buffer)

description

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

specific activity

≥100 units/mL

specific activity

≥800 units/mg protein

specific activity

20-50 units/mg protein (in glycine buffer)

specific activity

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

grade

Molecular Biology

grade

-

grade

-

grade

-

assay

≥95% (size exclusion chromatography)

assay

≥90%

assay

-

assay

-

biological source

Escherichia coli

biological source

-

biological source

Escherichia coli

biological source

-

suitability

suitable for molecular biology

suitability

-

suitability

-

suitability

-

application(s)

research use

application(s)

-

application(s)

-

application(s)

-


Clase de almacenamiento

10 - Combustible liquids



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