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Topo Enzymes

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TG2000EC
E. coli Topo IV is a type II topoisomerase that is encoded by two genes parC and parE in E. coli.  It is essential for decatenation and chromosomal segregation in E. coli; thus, topo IV tends to prefer intermolecular strand passing (catenating and decatenating reactions) over relaxation reactions.  It is…
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E. coli Topo IV is a type II topoisomerase that is encoded by two genes parC and parE in E. coli.  It is essential for decatenation and chromosomal segregation in E. coli; thus, topo IV tends to prefer intermolecular strand passing (catenating and decatenating reactions) over relaxation reactions.  It is overexpressed and purified for use.
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TG2005HRC
High purity, catalytically active Top1 Enzyme overexpressed in the baculovirus system and purified to single band homogeneity.  These preparations are cheaper than native topo I made from human tissue and offer excellent purity and high specific activity.
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TG2000H
We purify Human Topoisomerase IIα (Top2a) using a proprietary method developed by the staff at TopoGEN.  The purified enzyme is completely free of contamination and nucleases.  It alters linking number of a unique topoisomer in steps of two and the major polypeptide detected on SDS-PAGE is 170 kDa…
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We purify Human Topoisomerase IIα (Top2a) using a proprietary method developed by the staff at TopoGEN.  The purified enzyme is completely free of contamination and nucleases.  It alters linking number of a unique topoisomer in steps of two and the major polypeptide detected on SDS-PAGE is 170 kDa.      
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TG2005H-Y723F
TopoGEN now offers a catalytically inactive form of mutant human topoisomerase I purified to homogeneity (single band on SDS-PAGE).  The mutation is a single residue change at the active site tyrosine (which has been changed to phenylalanine).  This preparation is overexpressed in baculovirus and affinity purified as a…
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TopoGEN now offers a catalytically inactive form of mutant human topoisomerase I purified to homogeneity (single band on SDS-PAGE).  The mutation is a single residue change at the active site tyrosine (which has been changed to phenylalanine).  This preparation is overexpressed in baculovirus and affinity purified as a single band on SDS-PAGE of 100 kDa.  […]
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