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Recombinant Human Rad51 protein (His Tag)

Recombinant Human Rad51 protein (His Tag)
  • Recombinant Human Rad51 protein (His Tag)
  • Recombinant Human Rad51 protein (His Tag)

Price: ¥3600.00 ¥1200.00

Size:
100 μg 20 μg
  • 表达系统: E.coli
  • 蛋白编码: Q06609
别称
HsRAD51;DNA repair protein RAD51 homolog 1;RAD51;hRAD51
表达系统
E.coli
序列
Ala2-Asp339
蛋白编码
Q06609
种属
Human
计算分子量
37.1 kDa
表观分子量
37 kDa
标签
N-His
生物活性
Not validated for activity
纯度
> 90% as determined by reducing SDS-PAGE.
内毒素
< 10 EU/mg of the protein as determined by the LAL method
保存条件
Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
运输条件
This product is provided as lyophilized powder which is shipped with ice packs.
制剂
Lyophilized from a 0.2 μm filtered solution in PBS with 5% Trehalose and 5% Mannitol.
复溶方法
It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis.
背景
Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination. Binds to single and double-stranded DNA and exhibits DNA-dependent ATPase activity. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange (PubMed:26681308). Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3.
SDS-PAGE analysis of Human Rad51 proteins, 2μg/lane of Recombinant Human Rad51 proteins was resolved with SDS-PAGE under reducing conditions, showing bands at 37 KD.


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