Chimerx/Taq DNA Polymerase/1111/5,000 u

Source 

Thermus aquaticus

Description

• Thermostable enzyme of approximately 94 kDa from Thermus aquaticus
• Ultrapure, Recombinant protein

Applications

• Recommended for use in PCR and primer extension reactions at elevated temperatures to obtain a wide range of DNA products up to 10 Kb
• Taq DNA Polymerase enzyme replicates DNA at 74°C and exhibits a half-life of 40 minutes at 95°C (1, 2)
• Taq DNA Polymerase catalyzes the polymerization of nucleotides into duplex DNA in the 5→3 direction in the presence of magnesium ions
• Maintains the 5→3 exonuclease activity
• Lacks the 3→5 exonuclease activity

Reagents Supplied

10X Taq Buffer A
10X Taq Buffer B
10X Taq Buffer C 

Unit Definition 

One unit is defined as the amount of enzyme required to catalyze the incorporation of 10 nmoles of dNTP into acid-insoluble material in 30 minutes at 70°C

10X Reaction Buffer

10X Taq Buffer A (optimization buffer without MgCl₂): Buffer allows to optimize MgCl₂ concentration
10X Taq Buffer B (general application, up to 10 kb): Buffer contains 15 mM MgCl₂ and is optimized for use with 0.2 mM of each dNTP
10X Taq Buffer C (colored): 10X Taq Buffer B Enriched with two gel tracking dyes and a gel loading reagent; Enables direct loading of PCR products onto an agarose gel

Assay Conditions

25 mM Tris-HCl (pH 9.5 at 25°C)
50 mM KCl
10 mM MgCl₂
1 mM dithiothreitol
200 μM each of dCTP, dGTP, dTTP, and dATP (a mix of unlabeled and [α-³²P] dATP)
10 μg activated calf thymus DNA 
1 mg/ml bovine serum albumin
15 µg activated calf thymus DNA
Total reaction volume is 50 µl

Quality Control

All preparations are assayed for contaminating endonuclease, 3-exonuclease, and nonspecific single- and double-stranded DNase activities
Typical preparations are greater than 95% pure, as judged by SDS polyacrylamide gel electrophoresis

Storage Conditions

Store at -20°C
Shipped on dry ice 

Downloads

MSDS PDF

References

1. Chien, A., Edgar, D.B. and Trela, J.M. (1976) J. Bacteriol. 127, 1550
2. Kaledin, A.S., Sliusarenko, A.G. and Gorodetskii, S.I. (1980) Biokhimiya 45, 644