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D4545

Sigma-Aldrich

Taq DNA Polymerase from Thermus aquaticus

with 10× PCR reaction buffer without MgCl2

Synonym(s):

Taq polymerase, Taq polymerase enzyme

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.55

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

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

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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

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.

Unit Definition

One unit will incorporate 10 nmol of total dNTPs into acid-precipitable DNA in 30 min at 74 °C.

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.

Hazard Statements

Precautionary Statements

Hazard Classifications

Aquatic Chronic 3

WGK

WGK 1

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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
Nazim El-Andaloussi et al.
Molecular cell, 22(1), 51-62 (2006-04-08)
Alterations in DNA repair lead to genomic instability and higher risk of cancer. DNA base excision repair (BER) corrects damaged bases, apurinic sites, and single-strand DNA breaks. Here, a regulatory mechanism for DNA polymerase beta (Pol beta) is described. Pol
G Van Goethem et al.
Neurology, 63(7), 1251-1257 (2004-10-13)
To identify POLG mutations in patients with sensory ataxia and CNS features. The authors characterized clinical, laboratory, and molecular genetic features in eight patients from five European families. The authors conducted sequencing of coding exons of POLG, C10orf2 (Twinkle), and

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