Taq SSB (Active) Protein

Details zu Produkt Nr. ABIN2452212, Anbieter: Anmelden zum Anzeigen
Proteinname
Spezies
Thermus aquaticus
Quelle
Escherichia coli (E. coli)
Protein-Typ
Recombinant
Biologische Aktivität
Active
Applikation
Functional Studies (Func)
Optionen
Hersteller
Anmelden zum Anzeigen
Hersteller Produkt- Nr.
Anmelden zum Anzeigen
Produktmerkmale The absence of endonucleases and exonucleases was confirmed.
Reinheit > 95 % of protein determined by SDS-PAGE (CBB staining)
Proteinname
Hintergrund Thermus aquaticus derived single-stranded DNA binding protein (SSB) is a thermostable protein which binds to single-stranded DNA with high specificity but does not bind well to double-stranded DNA. It plays important roles in DNA replication and recombination. Thermus aquaticus SSB gene was expressed in E.Coli in large quantities and the protein was highly purified. MW is 30.0 kDa, same as that of the natural protein.
UniProt Q9KH06
Applikations-hinweise Stabilizes single-stranded DNA in DNA replication,repair,and recombination
Kommentare

Activity: Single-stranded DNA binding activity was confirmed.
Beschränkungen Nur für Forschungszwecke einsetzbar
Format Liquid
Konzentration 1.0 mg/mL
Buffer 50 mM Tris-HCl ( pH 8. 0), 200 mM NaCl, 0. 1 mM dithiothreitol, 0. 5 mM EDTA, 50 % glycerol
Konservierungs-mittel Dithiothreitol (DTT)
Vorsichtsmaßnahmen This product contains Dithiothreitol (DTT): a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung -20 °C
Bilder des Herstellers
SDS-PAGE (SDS) image for Taq SSB (Active) protein (ABIN2452212) Taq SSB (Active) protein
SDS-PAGE (SDS) image for Taq SSB (Active) protein (ABIN2452212) Taq SSB (Active) protein (Image 2)
Polymerase Chain Reaction (PCR) image for Taq SSB (Active) protein (ABIN2452212) Taq SSB (Active) protein (Image 3)
Polymerase Chain Reaction (PCR) image for Taq SSB (Active) protein (ABIN2452212) Taq SSB (Active) protein (Image 4)
Produkt verwendet in: Dabrowski, Olszewski, Piatek, Kur: "Novel thermostable ssDNA-binding proteins from Thermus thermophilus and T. aquaticus-expression and purification." in: Protein expression and purification, Vol. 26, Issue 1, pp. 131-8, 2002 (PubMed).

Haben Sie etwas anderes gesucht?