RuvB (Active) Protein
Origin: E. coli
Host: Escherichia coli (E. coli)
Native
SDS, Func, ELISA, WB
Active
(2 references)-
- Target
- RuvB
- Protein Type
- Native
- Biological Activity
- Active
- Origin
- E. coli
-
Source
- Escherichia coli (E. coli)
- Application
- SDS-PAGE (SDS), Functional Studies (Func), ELISA, Western Blotting (WB)
- Characteristics
- Full-length recombinant protein expressed in E.coli and highly purified by combined chromatography. RuvB protein is over 90 % by SDS-PAGE (CBB staining) pure.
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RuvB (AA 1-336), (full length) protein (His-SUMO Tag)
Origin: E. coli Host: Escherichia coli (E. coli) Recombinant > 90 % SDS
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- Application Notes
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1) Functional studies in vitro,RuvA and RuvB form a complex that promotes Holiday junction (a recombination intermediatae) branch-migration by using ATP hydrolysis energy. RuvB also has ATPase activity which is stimulated by RuvA and DNA.
2) SDS-PAGE (0. 2 g/lane)
3) Standard antigen for western blotting and ELISA - Restrictions
- For Research Use only
-
- Format
- Liquid
- Concentration
- 1.0 mg/mL
- Buffer
- 50 % glycerol, 10 mM Tris-HCl ( pH 7.5), 2 mM EDTA, 100 mM NaCl, 5 mM mercaptoethanol
- Storage
- -20 °C/-80 °C
- Storage Comment
- Upon arrival centrifuge briefly and store at -20 C or at -80 C for longer storage.
-
-
: "Processing the holliday junction in homologous recombination." in: Trends in biochemical sciences, Vol. 21, Issue 3, pp. 107-11, (1996) (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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: "Processing the holliday junction in homologous recombination." in: Trends in biochemical sciences, Vol. 21, Issue 3, pp. 107-11, (1996) (PubMed).
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- Target
- RuvB
- Background
- E. coli RuvB protein forms a complex with RuvA protein at the late stage of homologous recombination and recombination repair and binds specifically to the Holliday structure which is the intermediate of recombination, allowing the migration of Holliday junction using ATP hydrolysis energy and expands the heteroduplex region. RuvB forms a hexamer ring structure and surrounds the double chain DNA and covers RuvA tetramer bound to the Holliday junction from both sides. RuvB is a DNA motor protein which possesses the ATPase activity, activated by DNA and RuvA protein. Its molecular weight is 37 kD and forms a dimer in solution in the physiological condition. .
- UniProt
- P0A812
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