Description
T4 DNA Polymerase catalyzes the extension of a primed DNA template in the 5′→ 3′ direction. This enzyme exhibits a powerful 3′→ 5′ exonuclease activity, while lacking any inherent 5′→ 3′ exonuclease or strand displacement functions.
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Description: T4 DNA Polymerase catalyzes the extension of a primed DNA template in the 5' -> 3' direction. This enzyme exhibits a powerful 3' -> 5' exonuclease activity, while lacking any inherent 5' -> 3' exonuclease or strand displacement functions. Specific Activity: 5,555U/mg Application: - 3'-overhang removal to form blunt ends - 5'-overhang fill-in to form blunt ends - Single strand deletion for sub-cloning - Second strand synthesis in site-directed mutagenesis - Probe labeling using replacement synthesis Source: Purified from a strain of E. coli that expresses the recombinant T4 DNA Polymerase gene. Supplied in: 100 mM KPO4 1.0 mM Dithiothreitol 0.1 mM EDTA 50% Glycerol pH 6.5 @ 25°C Supplied With: 10x Blue Buffer 10x Blue Buffer: 500 mM NaCl 100 mM Tris-HCL 100 mM MgCl2 10 mM DTT pH 7.9 @ 25°C Unit Definition: One unit is defined as the amount of enzyme that will incorporate 10 nmol of dNTP into acid-precipitable material in 30 minutes at 37°C. Recommended Storage Conditions: -20ºC Reference: 1. Tabor, S. and Struhl, K. (1989) In DNA-Dependent DNA Polymerases. F. M. Ausebel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith and K. Struhl (Eds.), Current Protocols in Molecular Biology, pp. 3.5.10-3.5.12. 2. Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, (2nd Ed.), 5.44-5.47. 2. Dale, R., McClure, B. and Houchins, J. (1985) Plasmid, 13, 31-40. 3. Kunkel, T.A., Roberts, J.D. and Zakour, R.A. (1987) R. Wu and L. Grossman (Eds.), Methods Enzymol., 154, pp. 367-382. San Diego: Academic Press. 4. Panet, A., van de Sande, J.H., Loewen, P.C. and Khorana, H.G. (1973) Biochemistry, 12, 5045-5050. |
