概述

  • 产品名称Anti-RuvA抗体
    参阅全部 RuvA 一抗
  • 描述
    兔多克隆抗体to RuvA
  • 经测试应用适用于: WB, IPmore details
  • 种属反应性
    与反应: Escherichia coli
  • 免疫原

    Full length native protein (purified) (E. coli).

性能

应用

Our Abpromise guarantee covers the use of ab18576 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

应用 Ab评论 说明
WB Use at an assay dependent dilution. Predicted molecular weight: 22 kDa.
IP Use at an assay dependent dilution.

靶标

  • 相关性In Escherichia coli, the RuvA, RuvB and RuvC proteins are required for the late stages of homologous recombination and DNA repair. They are involved in processing the Holliday junction during homologous recombination. RuvA protein binds to both single-stranded and double-stranded DNA. RuvB protein has weak ATPase activity. RuvA bound to DNA greatly enhances ATPase activity of RuvB. UV-irradiation to supercoiled DNA further enhances the stimulatory effect of RuvA on the RuvB ATPase activity. In the presence of ATP the RuvA-RuvB complex has an activity that renatures cruciform structures formed by heating and gradually cooling supercoiled DNA with an inverted repeat. RuvA and RuvB promote branch migration whereas RuvC resolves junctions by endonucleolytic cleavage. Moreover RuvAB stimulate Holliday junction resolution by RuvC. The RuvA-RuvB complex interacts with an irregular conformation in damaged DNA and induces conformational changes in DNA using energy provided by ATP hydrolysis, so that it facilitates DNA repair, recombination and error prone replication. RuvABC proteins are responsible for the occurrence of DSBs at arrested replication forks. In cells proficient for RecBC, RuvAB is uncoupled from RuvC and DSBs may be prevented.
  • 数据库链接
    • 别名
      • Holliday junction ATP dependent DNA helicase ruvA antibody
      • Holliday junction DNA helicase RuvA antibody
      • Ruv A antibody

    Anti-RuvA antibody (ab18576)参考文献

    ab18576 has not yet been referenced specifically in any publications.

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