Recombinant Human Topoisomerase I protein
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Recombinant Human Topoisomerase I protein is a Human Full Length protein, in the 1 to 765 aa range, expressed in Baculovirus, with >95%, suitable for SDS-PAGE.
View Alternative Names
DNA topoisomerase 1, DNA topoisomerase I, TOP1
Reactivity data
Product details
1 unit equals 1 nanogram purified protein. 0.1 – 1 unit (ng) is sufficient for relaxing 0.5 μg of pBR322 supercoiled DNA in a 20 μl reaction.
Purified topo I has been used for in vitro transcriptional activation, pre-mRNA splicing/phosphorylation, DNA binding and DNA relaxation assays.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Topoisomerase I plays a significant role in the modulation of DNA topology ensuring proper chromosomal functions during cellular proliferation. It serves as a single polypeptide and does not require a companion for its activity unlike other topoisomerases that may function in complexes. The enzyme’s ability to relieve torsional stress in DNA is essential for maintaining genomic stability and facilitating the smooth progression of the replication fork.
Pathways
Topoisomerase I is vital for DNA replication and transcription processes. It works in concert with other proteins such as helicases and ligases to ensure efficient unwinding and rewinding of DNA strands. The enzyme participates in the DNA damage response pathway where it interacts with proteins like PARP1 to coordinate repair processes. Its action is important in both the S phase of the cell cycle where DNA synthesis occurs and in the G0 phase where cells are in a quiescent state.
Specifications
Form
Liquid
Additional notes
Purified by using an affinity column and FPLC chromatography.
General info
Function
Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. 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 then rotates around the intact phosphodiester bond on the opposing 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. Involved in the circadian transcription of the core circadian clock component BMAL1 by altering the chromatin structure around the ROR response elements (ROREs) on the BMAL1 promoter.
Sequence similarities
Belongs to the type IB topoisomerase family.
Post-translational modifications
Sumoylated. Lys-117 is the main site of sumoylation. Sumoylation plays a role in partitioning TOP1 between nucleoli and nucleoplasm. Levels are dramatically increased on camptothecin (CPT) treatment.. Phosphorylation at Ser-506 by CK2 increases binding to supercoiled DNA and sensitivity to camptothecin.
Subcellular localisation
Nucleus
Target data
Product promise
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