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Restriction enzymes, modifying enzymes, buffering solutions, inhibitors, and substrates for use in clinical, research, and general laboratory procedures.
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E. coli DNA Ligase catalyzes the formation of a phosphodiester bond between the 5'-phosphate and the 3'-hydroxyl of two adjacent DNA strands in duplex DNA with cohesive ends. It is not appreciably active on blunt-ended substrates. E. coli DNA Ligase uses NAD as a cofactor and can be heat-inactivated.
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Bst DNA Polymerase, Large Fragment is the portion of the Bacillus stearothermophilus DNA Polymerase protein that contains the 5' to 3' polymerase activity, but lacks 5' to 3' exonuclease activity.
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Topoisomerase I (E. coli) catalyzes the relaxation of negatively supercoiled DNA. Topoisomerase I has also been implicated in knotting and unknotting DNA and in linking complementary rings of single-stranded DNA into double-stranded rings. The intact holoenzyme is a 97 kDa protein.
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Exonuclease T (Exo T), also known as RNase T, is a single-stranded RNA or DNA specific nuclease that requires a free 3' terminus and removes nucleotides in the 3' to 5' direction. Exonuclease T can be used to generate blunt ends from RNA or DNA molecules that have 3 extensions.
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Enterokinase is a specific protease that cleaves after lysine at its cleavage site Asp-Asp-Asp-Asp-Lys. It will sometimes cleave at other basic residues, depending on the conformation of the protein substrate.
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Klenow Fragment (3' to 5' exo-) is an N-terminal truncation of DNA Polymerase I which retains polymerase activity, but has lost the 5' to 3' exonuclease activity and has mutations (D355A, E357A) which abolish the 3' to 5' exonuclease activity.
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Factor Xa cleaves after the arginine residue in its preferred cleavage site Ile-Glu/Asp-Gly-Arg. It will sometimes cleave at other basic residues, depending on the conformation of the protein substrate. The most common secondary site, among those that have been sequenced, is Gly-Arg.
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RNase H (Ribonuclease H ) is an endoribonuclease that specifically hydrolyzes the phosphodiester bonds of RNA which is hybridized to DNA. This enzyme does not digest single or double-stranded DNA.
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Inorganic pyrophosphatase (PPase) catalyzes the hydrolysis of inorganic pyrophosphate to form orthophosphate. A variety of metabolic reactions generate inorganic pyrophosphate as a reaction byproduct. Such reactions are rendered irreversible when the pyrophosphate is degraded by pyrophosphatase. RNA and DNA synthesis are examples of reactions that can be pulled far in the synthesis direction by the action of inorganic pyrophosphatase.
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