Terminal transferase (TdT) is a template-independent DNA polymerase that catalyzes the binding of deoxynucleotides to the 3' hydroxyl end of DNA molecules. Single-stranded and double-stranded DNA molecules with either sticky or blunt ends can all serve as substrates for TdT, with tailing lengths ranging from 5 to 300 nt.
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Cat. No.: TT-500 (for 500U)
Cat. No.: TT-2500 (for 2,500U)
This terminal transferase (TdT) has a molecular weight of 58.3 kDa and no 5' and 3' exonuclease activities. The addition of Co2+ to the reaction can improve the tailing efficiency. The enzyme is widely used in DNA 3' end addition homopolymer, DNA 3' end labeling using modified bases (such as ddNTP, DIG-dUTP), TdT-mediated dUTP nick end labeling technology (in situ detection of apoptosis), and other tests. The enzyme is tested free of DNA endonuclease and exonuclease contamination and RNase.
Oligonucleotide or DNA 3' hydroxyl end labeling
Synthesis of oligomeric strands of the same deoxynucleotide
The amount of enzyme required to catalyze the addition of 1 nmol dNTP to the 3' hydroxyl end of a polynucleotide within 60 min at 37°C is defined as an active unit.
1 x TdT Buffer
100 mM KCl, 30 mM Tris-acera, 0.05% (v/v) Triton X-100 (pH 7.5 at 25°C)
Stored at -20°C for 3 years.
75°C for 20 min.
The activity of Terminal Transferase can be lost by an appropriate amount of EDTA.
Metal ion chelators, higher concentrations of ammonium ions, chloride ions, iodine ions, and phosphate ions all have inhibitory effects on Terminal Transferase activity.
Only for research and not intended for treatment of humans or animals
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