Background: DNA Topoisomerase 1 releases the supercoiling and torsional tension of DNA introduced during DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. It introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone By similarity. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells.
Positive Control: Found in Endothelial cells.
Immunogen: Synthetic peptide made to human DNA Topoisomerase 1
Purification Method: Antigen Immunoaffinity Purification
Concentration: See vial for concentration
Formulation: Provided as solution in phosphate buffered saline with 0.08% sodium azide
References: 1. Oddou, P., et al. 'Monoclonal antibodies neutralizing mammalian DNA topoisomerase I activity.' Eur. J. Biochem. 1988, 177, 523-5292. Redinbo, M.R., et al. 'Novel insights into catalytic mechanism from a crystal structure of human topoisomerase I in complex with DNA.' Biochemistry 2000, 39, 6832-68403. Eisenreich, A., et al. 'Cdc2-like kinases and DNA topoisomerase I regulate alternative splicing of tissue factor in human endothelial cells.' Circ. Res. 2009, 104, 589-599
UniProt: P11387
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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