RuvC (Active) Protein

Details zu Produkt Nr. ABIN2452186, Anbieter: Anmelden zum Anzeigen
Proteinname
Spezies
Escherichia coli (E. coli)
2
Quelle
Escherichia coli (E. coli)
2
Protein-Typ
Native
Biologische Aktivität
Active
Applikation
Functional Studies (Func), SDS-PAGE (SDS), ELISA, Western Blotting (WB)
Optionen
Hersteller
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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)
Hintergrund 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
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.
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SDS-PAGE (SDS) image for RuvC (Active) protein (ABIN2452186) RuvC (Active) protein
SDS-PAGE (SDS) image for RuvC (Active) protein (ABIN2452186) RuvC (Active) protein (Image 2)
Produkt verwendet 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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