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Restriction enzymes, modifying enzymes, buffering solutions, inhibitors, and substrates for use in clinical, research, and general laboratory procedures.
T4 DNA Ligase is used for cloning of restriction enzyme generated DNA fragments and PCR products. It is also used for next-generation library preparation, joining linkers and adapters to cohesive or blunt-ended DNA, self-circularization of linear 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.
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.
TAB5 Alkaline Phosphatase is a heat labile alkaline phosphatase. It catalyzes the dephosphorylation of phosphomonoesters at both 5' and 3' ends of DNA and RNA molecules in a nonspecific manner. Additionally, it eliminates phosphate groups from the 5' and 3' positions of DNA, RNA, and dNTPs.
Klenow fragment (Exo-) is a mesophilic DNA polymerase deficient in both proofreading (3′→5′) and nick-translation (5′→3′) nuclease activities, with a moderate strand displacement activity during DNA synthesis.
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.
Taq DNA Ligase uses NAD+ as a cofactor to catalyze the formation of a phosphodiester bond in duplex DNA containing adjacent 5'-phosphoryl and 3'-hydroxyl termini.
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.
Endonuclease VIII from E. coli has dual functions as an N-glycosylase and an AP-lyase. It removes damaged pyrimidines from double-stranded DNA to create an AP site. The AP-lyase activity then cleaves at this site, resulting in a 5′ phosphate and a 3′ phosphate.