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T4 DNA Polymerase catalyzes the extension of a primed DNA template in the 5′→ 3′ direction. This enzyme exhibits a powerful 3′→ 5′ exonuclease activity; it lacks any inherent 5′→ 3′ exonuclease or strand displacement functions.
Pfu DNA Polymerase is a highly thermostable DNA polymerase from hyperthermophilic archaeum Pyrococcus furiosus.
T4 DNA Ligase catalyzes the formation of a phosphodiester bond between juxtaposed 5'-phosphate and 3'-hydroxyl termini in duplex DNA or RNA using ATP as a cofactor.
T7 DNA Ligase catalyzes the formation of a phosphodiester bond between a 5′ phosphate and a 3′ hydroxyl termini in duplex DNA. The enzyme joins blunt end and cohesive end termini as well as repair single stranded nicks in duplex DNA.
T4 RNA Ligase 1 catalyzes the ligation of a 5' phosphoryl-terminated nucleic acid donor to a 3' hydroxyl-terminated nucleic acid acceptor through the formation of a 3'→5' phosphodiester bond, with hydrolysis of ATP to AMP and PPi. Substrates include single-stranded RNA and DNA as well as dinucleoside pyrophosphates.
MCLAB’s truncated T4 RNA Ligase 2 was developed specifically for demanding Next-Generation RNA Sequencing applications. The truncated ligase 2 specifically ligates the adenylated 5´ end of an adapter to the 3´ end of RNA. The enzyme does not require ATP for ligation but does need an adenylated substrate. By not having an extra ATP in the reaction it dramatically reduces the amount of ligation between random RNA molecules.
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