|Other Names||Tyrosyl-DNA phosphodiesterase 1, Tyr-DNA phosphodiesterase 1, 314-, TDP1|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 3'-phosphodiester bond, giving rise to DNA with a free 3' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase I active site tyrosine residue. Hydrolyzes 3'-phosphoglycolates on protruding 3' ends on DNA double-strand breaks due to DNA damage by radiation and free radicals. Acts on blunt-ended double-strand DNA breaks and on single-stranded DNA. Has low 3'exonuclease activity and can remove a single nucleoside from the 3'end of DNA and RNA molecules with 3'hydroxyl groups. Has no exonuclease activity towards DNA or RNA with a 3'phosphate.|
|Cellular Location||Nucleus. Cytoplasm|
|Tissue Location||Ubiquitously expressed. Similar expression throughout the central nervous system (whole brain, amygdala, caudate nucleus, cerebellum, cerebral cortex, frontal lobe, hippocampus, medulla oblongata, occipital lobe, putamen, substantia nigra, temporal lobe, thalamus, nucleus accumbens and spinal cord) and increased expression in testis and thymus|
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The protein encoded by this gene is involved in repairingstalled topoisomerase I-DNA complexes by catalyzing the hydrolysisof the phosphodiester bond between the tyrosine residue oftopoisomerase I and the 3-prime phosphate of DNA. This protein mayalso remove glycolate from single-stranded DNA containing 3-primephosphoglycolate, suggesting a role in repair of free-radicalmediated DNA double-strand breaks. This gene is a member of thephospholipase D family and contains two PLD phosphodiesterasedomains. Mutations in this gene are associated with the diseasespinocerebellar ataxia with axonal neuropathy (SCAN1). Whileseveral transcript variants may exist for this gene, thefull-length natures of only two have been described to date. Thesetwo represent the major variants of this gene and encode the sameisoform.
Dexheimer, T.S., et al. Nucleic Acids Res. 38(7):2444-2452(2010)Chiang, S.C., et al. Cell Cycle 9(3):588-595(2010)Das, B.B., et al. EMBO J. 28(23):3667-3680(2009)Zhou, T., et al. DNA Repair (Amst.) 8(8):901-911(2009)Hoskins, J.M., et al. Pharmacogenomics 10(7):1139-1146(2009)
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