Recombinant Human TDP1 protein
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(2 Publications)
Recombinant Human TDP1 protein is a Human Full Length protein, in the 1 to 608 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
Tyrosyl-DNA phosphodiesterase 1, Tyr-DNA phosphodiesterase 1, TDP1
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human TDP1 protein (AB131921)
12.5% SDS-PAGE analysis of ab131921 stained with Coomassie Blue.
Reactivity data
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
TDP1 contributes significantly to the maintenance of genomic stability. It functions primarily as a DNA repair enzyme acting independently rather than as part of a protein complex. TDP1's ability to cleave phosphotyrosyl bonds makes it integral to processes that safeguard against DNA strand breaks induced by oxidative stress or other exogenous factors. Though not part of a complex its function is supported by the interaction with proteins like DNA polymerase which aids in the subsequent steps of DNA repair synthesis.
Pathways
TDP1 is involved in the DNA damage response and repair pathways. It collaborates heavily with the Base Excision Repair (BER) and the Single-Strand Break Repair (SSBR) pathways. TDP1 works alongside proteins like PARP1 facilitating the repair of single-strand DNA breaks which is critical for cell survival and prevention of mutations. Aphidicolin a known inhibitor of DNA polymerase can affect DNA synthesis steps that follow TDP1 activity indicating how interconnected these pathways are.
Specifications
Form
Liquid
General info
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.
Sequence similarities
Belongs to the tyrosyl-DNA phosphodiesterase family.
Post-translational modifications
Phosphorylated on serine and/or threonine residues, but not on tyrosine residues.
Subcellular localisation
Nucleus
Target data
Publications (2)
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Genes and environment : the official journal of the Japanese Environmental Mutagen Society 47:7 PubMed40155951
2025
Applications
Unspecified application
Species
Unspecified reactive species
The Journal of biological chemistry 299:104988 PubMed37392847
2023
Applications
Unspecified application
Species
Unspecified reactive species
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