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TDP2 / TTRAP Antibody (aa11-28)
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P |
|---|---|
| Primary Accession | O95551 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 41kDa |
| Dilution | IHC-P (5 µg/ml), WB (1:1000-1:5000), |
| Gene ID | 51567 |
|---|---|
| Other Names | Tyrosyl-DNA phosphodiesterase 2, Tyr-DNA phosphodiesterase 2, hTDP2, 3.1.4.-, 5'-tyrosyl-DNA phosphodiesterase, 5'-Tyr-DNA phosphodiesterase, ETS1-associated protein 2, ETS1-associated protein II, EAPII, TRAF and TNF receptor-associated protein, Tyrosyl-RNA phosphodiesterase, VPg unlinkase, TDP2, EAP2, TTRAP |
| Target/Specificity | Residues 11-28 (REAAEEEGEPEVKKRRLL) of human EAPII |
| Reconstitution & Storage | +4°C or -20°C, Avoid repeated freezing and thawing. |
| Precautions | TDP2 / TTRAP Antibody (aa11-28) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | TDP2 {ECO:0000303|PubMed:27060144} |
|---|---|
| Function | DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead- end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DNA double-strand breaks/DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'- phosphate termini that are ready for ligation (PubMed:27099339, PubMed:27060144). Thereby, protects the transcription of many genes involved in neurological development and maintenance from the abortive activity of TOP2. Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DSBs due to DNA damage by radiation and free radicals. Has preference for single-stranded DNA or duplex DNA with a 4 base pair overhang as substrate. Acts as a regulator of ribosome biogenesis following stress. Has also 3'-tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. Constitutes the major if not only 5'-tyrosyl-DNA phosphodiesterase in cells. Also acts as an adapter by participating in the specific activation of MAP3K7/TAK1 in response to TGF-beta: associates with components of the TGF-beta receptor-TRAF6-TAK1 signaling module and promotes their ubiquitination dependent complex formation. Involved in non-canonical TGF-beta induced signaling routes. May also act as a negative regulator of ETS1 and may inhibit NF-kappa-B activation. |
| Cellular Location | Nucleus. Nucleus, PML body Nucleus, nucleolus. Cytoplasm Note=Localizes to nucleolar cavities following stress; localization to nucleolus is dependent on PML protein. |
| Tissue Location | Widely expressed (PubMed:10764746). Highly expressed in various brain regions, including the frontal and occipital lobes, the hippocampus, the striatum and the cerebellum (PubMed:24658003). |
| Volume | 50 µl |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. Hydrolyzes 5'- phosphoglycolates on protruding 5' ends on DNA double-strand breaks (DSBs) due to DNA damage by radiation and free radicals. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation. Has preference for single-stranded DNA or duplex DNA with a 4 base pair overhang as substrate. Has also 3'- tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. Constitutes the major if not only 5'- tyrosyl-DNA phosphodiesterase in cells. Also acts as a 5'-tyrosyl- RNA phosphodiesterase following picornavirus infection: its activity is hijacked by picornavirus and acts by specifically cleaving the protein-RNA covalent linkage generated during the viral genomic RNA replication steps of a picornavirus infection, without impairing the integrity of viral RNA. Also acts as an adapter by participating in the specific activation of MAP3K7/TAK1 in response to TGF-beta: associates with components of the TGF- beta receptor-TRAF6-TAK1 signaling module and promotes their ubiquitination dependent complex formation. Involved in non- canonical TGF-beta induced signaling routes. May also act as a negative regulator of ETS1 and may inhibit NF-kappa-B activation. Acts as a regulator of ribosome biogenesis following stress.
References
Pype S.,et al.J. Biol. Chem. 275:18586-18593(2000).
Pei H.,et al.Oncogene 22:2699-2709(2003).
Hu R.-M.,et al.Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Mungall A.J.,et al.Nature 425:805-811(2003).
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