RuvA Protein
Origin: E. coli
Host: Escherichia coli (E. coli)
Recombinant
> 90 % by SDS-PAGE (CBB staining)
Func
Active
(2 references)-
- Target See all RuvA products
- RuvA
- Protein Type
- Recombinant
- Biological Activity
- Active
- Origin
- E. coli
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Source
- Escherichia coli (E. coli)
- Application
- Functional Studies (Func)
- Characteristics
- The product is a recombinant protein abundantly expressed by E. coli and purified by methods such as chromatography. The molecular weight is 22 kD and even in solution, it binds to the Holliday structure and form a tetramer.
- Purity
- > 90 % by SDS-PAGE (CBB staining)
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RuvA (AA 1-203), (full length) protein (His-SUMO Tag)
Origin: E. coli Host: Escherichia coli (E. coli) Recombinant > 90 % SDS
RuvA (Active) proteinOrigin: E. coli Host: Escherichia coli (E. coli) Native Func Active
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- Application Notes
-
1) Functional as Holliday junction specific binding protein,which promotes Holliday-junction branch migration in combination with RuvB protein.
2) For SNP analysis (Genome Research 13:1754-1764 PMID: 12840050). - Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 2.7 mg/mL
- Buffer
- 50 % glycerol, 10 mM Tris-HCl ( pH 7.5), 2 mM EDTA, 100 mM NaCl, 5 mM mercaptoethanol
- Storage
- -20 °C
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-
: "Direct observation of DNA rotation during branch migration of Holliday junction DNA by Escherichia coli RuvA-RuvB protein complex." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 103, Issue 31, pp. 11544-8, (2006) (PubMed).
: "Escherichia coli RuvA and RuvB proteins specifically interact with Holliday junctions and promote branch migration." in: Genes & development, Vol. 6, Issue 11, pp. 2214-20, (1992) (PubMed).
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: "Direct observation of DNA rotation during branch migration of Holliday junction DNA by Escherichia coli RuvA-RuvB protein complex." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 103, Issue 31, pp. 11544-8, (2006) (PubMed).
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- Target
- RuvA
- Abstract
- RuvA Products
- Background
- E. coli RuvA protein binds specifically to the Holliday structure which is the intermediate of recombination at the late stage of homologous recombination and recombination repair and forms a complex with RuvB motor protein allowing the migration of Holliday junction using ATP hydrolysis energy and expands the heteroduplex region. In solution, it forms a tetramer and binds to the cross-like DNA of the Holliday junction from below and above holding it in between.
- UniProt
- P0A809
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