RuvC (Active) Protein

Details for Product No. ABIN2452186, Supplier: Log in to see
Protein Name
Escherichia coli (E. coli)
Escherichia coli (E. coli)
Protein Type
Biological Activity
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. RuvC protein purity is over 90 % by SDS-PAGE (CBB staining)
Background E. coli RuvC protein (19 kDa) is a structurally specific endonuclease which binds specifically to the Holliday structure, an intermediate of recombination, at the late stage of homologous recombination and recombination repair and introduces a nick in the symmetrical point of the Holliday junction leaving and resolving the recombinant. Functional form is dimmer.
UniProt P0A814
Research Area Chromatin and Nuclear Signaling, DNA/RNA
Application Notes 1) Functional studies in vitro. RuvC cleaves recombination intermediate at Holliday Junction.
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 RuvC (Active) protein (ABIN2452186) RuvC (Active) protein
Product cited in: Murayama, Kurokawa, Mayanagi, Iwasaki: "Formation and branch migration of Holliday junctions mediated by eukaryotic recombinases." in: Nature, Vol. 451, Issue 7181, pp. 1018-21, 2008 (PubMed).

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, Shiba, Nakata, Shinagawa: "Escherichia coli RuvC protein is an endonuclease that resolves the Holliday structure." in: The EMBO journal, Vol. 10, Issue 13, pp. 4381-9, 1992 (PubMed).

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