T7428
Topoisomerase I from wheat germ
buffered aqueous glycerol solution
别名:
DNA relaxing enzyme, Topo I
等级
Molecular Biology
表单
buffered aqueous glycerol solution
分子量
97 kDa
异质活性
RNase and DNase, none detected
运输
dry ice
储存温度
−70°C
一般描述
Topoisomerase I relaxes supercoiled DNA molecules. The enzyme initiates transient breakages and rejoins of phosphodiester bonds in superhelical turns of closedcircular dsDNA.
应用
Suitable for:
- Analsis of degree of DNA supercoiling
- Forming knots and circles in single stranded DNA
- Converting complementary single stranded DNA to double stranded, circular forms
- Rejoining nicks in double-stranded DNA
生化/生理作用
Topoisomerase I relaxes supercoiled DNA molecules. The enzyme initiates transient breakages and rejoins of phosphodiester bonds in superhelical turns of closed-circular DNA. Enzyme activity is independent of right- and left-handed superhelices.
其他说明
One unit will convert 1μg of supercoiled pGEM9Zf(−) plasmid DNA to the relaxed form in 30 min at 37 °C.
To preserve enzyme activity, avoid multiple freeze-thaw cycles and frequent temperature variations.
Topoisomerase I is supplied in a solution of 50 mM Tris-HCl, pH 7.9, 1 mM EDTA, 1 mM DTT, 0.5 M NaCl and 50% glycerol (v/v).
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
新产品
此项目有
P D Foglesong et al.
BioTechniques, 13(3), 402-404 (1992-09-01)
Supercoiled and relaxed DNA were resolved electrophoretically in the presence of 0.5 micrograms/ml ethidium bromide. Under these conditions the Gaussian distributions of topological isomers of both supercoiled and relaxed DNA migrated as discrete bands. The separation of these DNAs was
J C Wang
Annual review of biochemistry, 65, 635-692 (1996-01-01)
The various problems of disentangling DNA strands or duplexes in a cell are all rooted in the double-helical structure of DNA. Three distinct subfamilies of enzymes, known as the DNA topoisomerases, have evolved to solve these problems. This review focuses
Martin Conda-Sheridan et al.
Journal of medicinal chemistry, 56(1), 182-200 (2012-12-25)
Tyrosyl-DNA phosphodiesterase I (Tdp1) plays a key role in the repair of damaged DNA resulting from the topoisomerase I (Top1) inhibitor camptothecin and a variety of other DNA-damaging anticancer agents. This report documents the design, synthesis, and evaluation of new
Markus G Rudolph et al.
Nucleic acids research, 41(2), 1058-1070 (2012-12-05)
Reverse gyrase is an ATP-dependent topoisomerase that is unique to hyperthermophilic archaea and eubacteria. The only reverse gyrase structure determined to date has revealed the arrangement of the N-terminal helicase domain and the C-terminal topoisomerase domain that intimately cooperate to
Lyudmila Yakovleva et al.
Biochemistry, 52(5), 984-991 (2013-01-16)
Vaccinia DNA topoisomerase IB (TopIB) relaxes supercoils by forming and resealing a covalent DNA-(3'-phosphotyrosyl(274))-enzyme intermediate. Conserved active site side chains promote the attack of Tyr274 on the scissile phosphodiester via transition state stabilization and general acid catalysis. Two essential side
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