RuvB (Active) Protein

Details for Product No. ABIN2452184, Supplier: Log in to see
Protein Name
Origin
Escherichia coli (E. coli)
2
Source
Escherichia coli (E. coli)
2
Protein Type
Native
Biological Activity
Active
Application
Functional Studies (Func), SDS-PAGE (SDS), ELISA, Western Blotting (WB)
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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.
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
Research Area Chromatin and Nuclear Signaling, DNA/RNA, Bacteria
Application Notes 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.
Supplier Images
SDS-PAGE (SDS) image for RuvB (Active) protein (ABIN2452184) RuvB (Active) protein
Product cited in: Shinagawa, Iwasaki: "Processing the holliday junction in homologous recombination." in: Trends in biochemical sciences, Vol. 21, Issue 3, pp. 107-11, 1996 (PubMed).

Iwasaki, Takahagi, Nakata, Shinagawa: "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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