EAPII Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| FC, IF, IHC-P, WB, E |
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Primary Accession | O95551 |
Other Accession | NP_057698 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 40930 Da |
Antigen Region | 246-272 aa |
Gene ID | 51567 |
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Other Names | Tyrosyl-DNA phosphodiesterase 2, Tyr-DNA phosphodiesterase 2, hTDP2, 314-, 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 | This EAPII antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 246-272 amino acids from the C-terminal region of human EAPII. |
Dilution | IF~~1:10~50 WB~~1:1000 IHC-P~~1:10~50 FC~~1:10~50 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | EAPII Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | TDP2 {ECO:0000303|PubMed:27060144} |
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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:27060144, PubMed:27099339). 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). |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a member of a superfamily of divalent cation-dependent phosphodiesterases. The encoded protein associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor associated factors (TRAFs), and inhibits nuclear factor-kappa-B activation. This protein has sequence and structural similarities with APE1 endonuclease, which is involved in both DNA repair and the activation of transcription factors.
References
Shimada, M., et al. Hum. Genet. 128(4):433-441(2010)
Wang, B.Y., et al. Mol. Biol. Rep. 37(6):2809-2816(2010)
Iijima, M., et al. Neurology 73(17):1348-1352(2009)
Cortes Ledesma, F., et al. Nature 461(7264):674-678(2009)
Zhang, J.Q., et al. Biochem. Biophys. Res. Commun. 387(2):256-260(2009)
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