Anti-TDP1 / Tyrosyl-DNA phosphodiesterase 1

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. TDP1 antibody detects Tyrosyl-DNA phosphodiesterase 1, a DNA repair enzyme that removes covalently trapped topoisomerase I-DNA complexes and repairs DNA single-strand breaks. The UniProt recommended name is Tyrosyl-DNA phosphodiesterase 1 (TDP1). This enzyme maintains genome stability by resolving abortive topoisomerase I intermediates generated during DNA replication and transcription.Functionally, TDP1 antibody identifies a 608-amino-acid nuclear enzyme that hydrolyzes the phosphodiester bond linking tyrosine residues of topoisomerase I to the 3? end of DNA. TDP1 also processes other blocked DNA termini generated by oxidative damage or chemotherapeutic agents. Its catalytic mechanism involves two histidine residues acting in a transesterification reaction, forming a transient covalent intermediate. TDP1 cooperates with PARP1 and XRCC1 in the single-strand break repair pathway to restore DNA integrity.The TDP1 gene is located on chromosome 14q32.11 and is expressed in a broad range of tissues, with highest levels in brain, thymus, and testis. Expression increases in response to DNA damage and genotoxic stress, indicating a role in stress-induced DNA repair. TDP1 activity supports genomic maintenance in neurons, where oxidative DNA damage is frequent.Pathologically, mutations in TDP1 cause spinocerebellar ataxia with axonal neuropathy (SCAN1), a rare neurodegenerative disorder characterized by progressive motor impairment and neuronal DNA repair deficiency. In cancer, TDP1 confers resistance to topoisomerase I inhibitors such as camptothecin and topotecan by removing drug-stabilized cleavage complexes. Research using TDP1 antibody supports studies in DNA repair, cancer pharmacology, and neurodegeneration.TDP1 antibody is validated for western blotting, immunofluorescence, and immunohistochemistry to detect DNA repair enzymes. NSJ Bioreagents provides TDP1 antibody reagents optimized for research in genomic maintenance, DNA damage response, and therapeutic resistance mechanisms.Structurally, Tyrosyl-DNA phosphodiesterase 1 consists of two domains forming an alpha/beta sandwich fold that positions catalytic histidine residues in the active site. The enzyme's flexible loops accommodate diverse DNA substrates, and phosphorylation or SUMOylation modulates its repair activity. This antibody facilitates investigation of TDP1's role in DNA repair, topoisomerase regulation, and neuroprotection.