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E. coli DNA Ligase is a NAD+-dependent enzyme that catalyzes the formation of phosphodiester bonds between complementary 3'-hydroxyl and 5'-phosphoryl termini of dsDNA.
T3 DNA Ligase catalyzes the formation of a phosphodiester bond between a 5′ phosphate and a 3′ hydroxyl terminus in duplex DNA. The enzyme joins blunt ends and cohesive ends as well as repair single stranded nicks in duplex DNA.
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.
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.
T4 RNA Ligase 2, also known as T4 Rnl2 (gp24.1), has both intermolecular and intramolecular RNA strand joining activity. Unlike T4 RNA Ligase 1, T4 RNA Ligase 2 is much more active joining nicks on double stranded RNA than on joining the ends of single stranded RNA. The enzyme requires an adjacent 5´ phosphate and 3´ OH for ligation.
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.
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.
Taq DNA Ligase catalyzes the formation of a phosphodiester bond in duplex DNA containing adjacent 5'-phosphoryl and 3'-hydroxyl termini, using NAD+ as a cofactor.
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