KEM0032
Terminal deoxynucleotidyl Transferase (TdT)
Ultra-pure enzyme for nucleic acid modifications
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About This Item
Recommended Products
grade
for molecular biology
Assay
>99% (SDS-PAGE)
form
buffered aqueous solution
specific activity
27,400 U/mg
concentration
20,000 U/mL
shipped in
dry ice
storage temp.
−20°C
General description
Terminal deoxynucleotidyl transferase (TdT) is a template-independent DNA polymerase that catalyzes the addition of deoxynucleotides to the 3′ hydroxyl terminus of single or double stranded DNA molecules. The presence of 1 mM Co2+ stimulates the tailing of the 3′-ends of DNA fragments. This construct is sold as an N-terminal truncation of the terminal transferase gene attached to an N-terminal fusion tag.
Application
Suitable for:
- Homopolymeric tailing to the 3′ OH
- TUNEL assay
- 5′-RACE
- Labeling of 3′ ends
Features and Benefits
- Ultra-purification process for ultimate enzyme performance
- Highest quality specifications for ultimate product consistency
- Undetectable DNA and nuclease contamination
Components
Supplied with:KEM0043B (10X Green Buffer)KEM0045B (2.5 mM CoCl2
Unit Definition
1 unit is defined as the amount of polymerase required to convert 1 nmol of dTTPs into acid insoluble material in 1 hour at 37° C.
Physical form
Supplied in 50 mM KPO4, 100 mM NaCl, 1.0 mM DTT, 0.1 mM EDTA, 0.1% Triton™ X-100, and 50% glycerol at pH 7.3 @ 25° C.
Other Notes
Source of protein: An E. coli strain that carries the cloned terminal transferase gene from calf thymus.
Unit size: 6,000 U
Legal Information
Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow
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Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Aquatic Chronic 3 - Carc. 1B
Storage Class Code
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
Regulatory Information
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Laure Rittié et al.
Journal of cell communication and signaling, 2(1-2), 25-45 (2008-09-04)
Since molecular cloning has become routine laboratory technique, manufacturers offer countless sources of enzymes to generate and manipulate nucleic acids. Thus, selecting the appropriate enzyme for a specific task may seem difficult to the novice. This review aims at providing
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