重组thermus aquaticus RecA蛋白(ab123228)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Active: Yes
- Suitable for: Functional Studies, SDS-PAGE, Electron Microscopy
描述
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产品名称
重组thermus aquaticus RecA蛋白
参阅全部 RecA 蛋白酶 -
生物活性
The activity of single-stranded DNA-dependent ATPase was confirmed.
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纯度
> 90 % SDS-PAGE. -
表达系统
Escherichia coli -
Accession
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蛋白长度
Full length protein -
无动物成分
No -
性质
Recombinant -
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种属
Thermus aquaticus -
预测分子量
37 kDa -
氨基酸
1 to 340 -
额外的序列信息
This Protein is from Thermus aquaticus
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技术指标
Our Abpromise guarantee covers the use of ab123228 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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应用
Functional Studies
SDS-PAGE
Electron Microscopy
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形式
Liquid -
Concentration information loading...
制备和贮存
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稳定性和存储
Shipped at 4°C. Store at -20°C.
pH: 6.5
Constituents: 0.79% Tris HCl, 0.03% EDTA, 50% Glycerol (glycerin, glycerine), 1.17% Sodium chlorideThis product is an active protein and may elicit a biological response in vivo, handle with caution.
常规信息
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别名
- DNA strand exchange and recombination protein with protease and nuclease activity
- lexB
- Protein recA
see all -
相关性
RecA in E.coli can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with lexA causing its activation and leading to its autocatalytic cleavage. -
细胞定位
Cytoplasmic
实验方案
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
数据表及文件
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SDS download
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Datasheet download
文献 (2)
ab123228 被引用在 2 文献中.
- Shigemori Y et al. Multiplex PCR: use of heat-stable Thermus thermophilus RecA protein to minimize non-specific PCR products. Nucleic Acids Res 33:e126 (2005). PubMed: 16087733
- Angov E & Camerini-Otero RD The recA gene from the thermophile Thermus aquaticus YT-1: cloning, expression, and characterization. J Bacteriol 176:1405-12 (1994). PubMed: 8113181