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
Forschungsgebiet Chromatin and Nuclear Signaling, DNA/RNA
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.
Bilder des Herstellers
SDS-PAGE (SDS) image for RuvC (Active) protein (ABIN2452186) RuvC (Active) protein
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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