SDS-PAGE (SDS), Functional Studies (Func), ELISA, Western Blotting (WB)
Produktmerkmale
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)
RuvC
Spezies: E. coli
Wirt: Escherichia coli (E. coli)
Recombinant
> 90 %
SDS
Applikationshinweise
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
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Konzentration
1.0 mg/mL
Buffer
50 % glycerol, 10 mM Tris-HCl ( pH 7.5), 2 mM EDTA, 100 mM NaCl, 5 mM mercaptoethanol
Lagerung
-20 °C/-80 °C
Informationen zur Lagerung
Upon arrival centrifuge briefly and store at -20 C or at -80 C for longer storage.
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).
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.