Taq DNA Polymerase

Downloads

MSDS PDF -Current Lot

Reagents Supplied

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

Source 

Thermus aquaticus

Description

• Taq DNA Polymerase is a thermostable enzyme of approximately 94 kDa from Thermus aquaticus
• Ultrapure, Recombinant protein

Applications

• Taq DNA Polymerase is recommended for use in PCR and primer extension reactions at elevated temperatures to obtain a wide range of DNA products up to 10 Kb
• The enzyme replicates DNA at 74°C and exhibits a half-life of 40 minutes at 95°C (1,2)
• 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

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

10 x Reaction Buffer

10 x Taq Buffer A (optimization buffer without MgCl₂): the buffer allows to optimize MgCl₂ concentration
10 x Taq Buffer B (general application, up to 10 kb): the buffer contains 15 mM MgCl₂ and is optimized for use with 0.2 mM of each dNTP
10 x Taq Buffer C (colored): 10 x Taq Buffer B enriched with two gel tracking dyes and a gel loading reagent. The buffer 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 

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