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生物来源
Escherichia coli
质量水平
重组
expressed in E. coli
等级
for molecular biology
描述
Recombinant, expressed in E.coli
方案
≥95% (size exclusion chromatography)
表单
buffered aqueous solution
比活
≥100 units/mL
保质期
2 yr at -20 °C ((retest))
分子量
19.7 kDa
储存条件
OK to freeze
浓度
≥100 units/mL
颜色
colorless
最佳pH
9.0 (25 °C)
pH值(酸碱度)
8.0 (25 °C)
溶解性
soluble
water: miscible
适用性
suitable for molecular biology
UniProt登记号
应用
research use
异质活性
DNAse, none detected
RNAse, none detected
Nickase, none detected
运输
dry ice
储存温度
-10 to -25°C
一般描述
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).
应用
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.
生化/生理作用
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.
特点和优势
This product has a purity minimum of 95% (SEC-HPLC) and an activity minimum of 100 units/mL to enhance RNA yield during transcription.
单位定义
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.
外形
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.
储存分类代码
10 - Combustible liquids
WGK
WGK 1
法规信息
新产品
历史批次信息供参考:
分析证书(COA)
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
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
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
Microbial inorganic pyrophosphatases.
Microbiological reviews, 47(2), 169-178 (1983-06-01)
Trends in biochemical sciences, 17(7), 262-266 (1992-07-01)
Soluble inorganic pyrophosphatases (PPases) are essential enzymes that are important for controlling the cellular levels of inorganic pyrophosphate (PPi). Although prokaryotic and eukaryotic PPases differ substantially in amino acid sequence, recent evidence now demonstrates clearly that PPases throughout evolution show
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