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Restriction enzymes, modifying enzymes, buffering solutions, inhibitors, and substrates for use in clinical, research, and general laboratory procedures.
T7 DNA Ligase is an ATP-dependent enzyme from bacteriophage T7 that catalyzes phosphodiester bond formation between 5′ phosphate and 3′ hydroxyl termini of duplex DNA.
T4 RNA Ligase I (gp63) catalyzes the ATP-dependent ligation of single-stranded nucleic acids by joining a 5′ phosphate to a 3′ hydroxyl. It is most efficient at ligating the 3′-OH of RNA to the 5′-phosphate of RNA or DNA in single-stranded contexts.
Exonuclease I (Exo I), is a highly processive single-stranded DNA-specific exonuclease which removes mono- and dinucleotides from the 3' end of single-stranded DNA molecules (3' to 5' exonuclease activity) leaving double-stranded molecules and the 5' end of single stranded molecules intact.
Thermolabile Uracil-DNA Glycosylase (UDG), originating from the species Gadus morhua, removes uracil from DNA by hydrolyzing the N-glycosylic bond between the deoxyribose and the base leaving an AP (apurinic or apyrimidinic) site.
T3 DNA Ligase catalyzes the formation of a phosphodiester bond between a 5' phosphate and a 3' hydroxyl termini in duplex DNA; joining blunt and cohesive end termini as well as repairing single stranded nicks in duplex DNA.