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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.55
MDL number:
Biological source:
enzyme from bacterial (Thermus Aquaticus)
Recombinant:
expressed in E. coli
Concentration:
5 units/μL
biological source
enzyme from bacterial (Thermus Aquaticus)
Quality Level
recombinant
expressed in E. coli
form
liquid
usage
sufficient for 1500 reactions, sufficient for 250 reactions, sufficient for 50 reactions, sufficient for 5000 reactions
feature
dNTPs included: no, hotstart: no, Standard PCR
concentration
5 units/μL
technique(s)
PCR: suitable
color
colorless
input
purified DNA
suitability
suitable for PCR and automated sequencing reactions
application(s)
agriculture
shipped in
wet ice
storage temp.
−20°C
General description
Taq polymerase is a thermostable DNA polymerase named after the thermophilic bacterium Thermus aquaticus. A stable deoxyribonucleic acid (DNA) polymerase (with a temperature optimum of 80°C) has been purified from the extreme thermophile Thermus aquaticus. The enzyme is free from phosphomonoesterase, phosphodiesterase and single-stranded exonuclease activities. Maximal activity of the enzyme needs all four deoxyribonucleotides and activated calf thymus DNA.
Application
Taq DNA Polymerase from Thermus aquaticus has been used:
- in the process of DNA extraction (during gene amplification and sequencing)
- in genotyping
- in polymerase chain reaction (PCR) to study the constitutive production of epithelial neutrophil activating peptide 78 (ENA-78) and interleukin-8 (IL-8)
- for amplification of RNA from primary endothelial cells by conventional PCR
Biochem/physiol Actions
Taq polymerase catalyzes oligonucleotide primer-driven, DNA template dependent incorporation of dNTPs into complimentary DNA strands. It displays both 5′ to 3′ polymerase and exonuclease activities.
Features and Benefits
- MgCl2 provided in a separate tube to allow MgCl2 optimization
- Can withstand repeated heating to 95 °C without significant loss of activity
Packaging
Taq DNA Polymerase with 10× reaction buffer without MgCl2. Includes a separate tube of 25 mM MgCl2
Taq DNA polymerase comes with the choice of an optimized 10× reaction buffer including MgCl2 (D1806) or a 10× reaction buffer without MgCl2 plus a separate tube of MgCl2 for titration (D4545). The latter option may be necessary to determine optimal conditions for amplification.
Other Notes
One unit will incorporate 10 nmol of total dNTPs into acid-precipitable DNA in 30 min at 74 °C.
Taq DNA Polymerase is a specialized thermostable enzyme isolated from the thermophilic bacterium Thermus aquaticus. The recombinant form of this enzyme is expressed in E. coli. This 94 kDa protein shows no detectable levels of contaminating endonucleases or exonucleases by SDS-PAGE. It has both 5′→3′ polymerase and exonuclease activity.
Legal Information
Use of this product is covered by one or more of the following US patents and corresponding patent claims outside the US: US 8,404,464 and US 7,972,828. The purchase of this product includes a limited, non-transferable immunity from suit under the foregoing patent claims.
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flash_point_f
Not applicable
hcodes
pcodes
Hazard Classifications
Aquatic Chronic 3
Storage Class
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_c
Not applicable
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Related Content
A Chien et al.
Journal of bacteriology, 127(3), 1550-1557 (1976-09-01)
A stable deoxyribonucleic acid (DNA) polymerase (EC 2.7.7.7) with a temperature optimum of 80 degrees C has been purified from the extreme thermophile Thermus aquaticus. The enzyme is free from phosphomonoesterase, phosphodiesterase and single-stranded exonuclease activities. Maximal activity of the
Nick A Bersinger et al.
Fertility and sterility, 89(5 Suppl), 1530-1536 (2007-09-01)
To analyze the constitutive production of epithelial neutrophil activating peptide 78 (ENA-78) and interleukin-8 (IL-8) by epithelial cells and the response of these cells to cytokine stimulation. In vitro study using eutopic endometrial tissue. University hospital. Cycling women undergoing laparoscopy
Slobodan Jergic et al.
The EMBO journal, 32(9), 1322-1333 (2013-02-26)
Processive DNA synthesis by the αεθ core of the Escherichia coli Pol III replicase requires it to be bound to the β2 clamp via a site in the α polymerase subunit. How the ε proofreading exonuclease subunit influences DNA synthesis