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TDP2 encodes a member of a superfamily of divalent cation-dependent phosphodiesterases. Additionally we are shipping TDP2 Antibodies (88) and many more products for this protein.
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Both the genome instability and cell death of MRE11 (show MRE11A Proteins)-null and MRE11 (show MRE11A Proteins)-mutated H129N cells are significantly reversed by overexpression of Tdp2, an enzyme that eliminates covalent Top2 (show TOP2A Proteins) conjugates; thus, the essential role of Mre11 (show MRE11A Proteins) nuclease (show DCLRE1C Proteins) activity is likely to remove the DNA lesions.
Study revealed a post-translational regulation of TDP2 activity and discovered a new role of ERK3 (show MAPK4 Proteins) in increasing cancer cells' DNA damage response and chemoresistance to Top2 (show TOP2A Proteins) inhibitors.
Data show that DNA-repair enzyme (show LIG4 Proteins) TDP2 knockdown in HepG2 cells significantly delays the conversion of relaxed circular DNA (RC-DNA) to covalently closed circular (ccc) DNA.
This article summarizes and compares the biochemistry, functions, and post-translational regulation of TDP1 (show TDP1 Proteins) and TDP2, as well as the relevance of TDP1 (show TDP1 Proteins) and TDP2 as determinants of response to anticancer agents
Proteolytic degradation of Top2 (show TOP2A Proteins) enables the processing of Top2 (show TOP2A Proteins).DNA and Top2 (show TOP2A Proteins).RNA covalent complexes by TDP2.
TDP2 protects transcription from abortive topoisomerase activity and is required for normal neural function.
Mutations in the 5'-tyrosyl-DNA phosphodiesterase activity of TTRAP,in particular TTRAP(E152A), showed decreased inhibitory activity on cell growth.
Magnesium is indispensable for a 5'-tyrosyl DNA phosphodiesterase activity.
VPg unlinkase activity in different mammalian cell lines correlates with their differential expression of TDP2.
Biochemical characterization of human tyrosyl-DNA phosphodiesterase 2 (TDP2/TTRAP): a Mg(2 (show MUC7 Proteins)+)/Mn(2+)-dependent phosphodiesterase specific for the repair of topoisomerase cleavage complexes.
The results collectively provide a structural mechanism for Tdp2 engagement of heterogeneous DNA damage that causes Top2 (show TOP2 Proteins) poisoning.
data show that TDP2 activity potentiates enterovirus infections and, in the case of coxsackievirus B3, is a required host function following virus infection of mouse cells
our data reveal TDP2-mediated error-free NHEJ as an efficient and accurate mechanism to repair TOP2 (show TOP2 Proteins)-induced DSBs
Evidence implicates Tdp2 in the repair of Top1 (show TOP1 Proteins)-mediated DNA damage in cultured cells and in vivo, in the absence of Tdp1 (show TDP1 Proteins).
the protein associates with TGF-beta (show TGFB1 Proteins) receptors and components of the TRAF6 (show TRAF6 Proteins)-TAK1 (show NR2C2 Proteins) signaling module
although the role of Smad (show SMAD1 Proteins) proteins in mediating Nodal signaling is well-documented, the functional characterization of Ttrap provides insight into a novel Smad (show SMAD1 Proteins) partner that plays an essential role in the fine-tuning of this signal transduction cascade
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.
, 5'-tyrosyl-DNA phosphodiesterase
, ETS1-associated protein 2
, ETS1-associated protein II
, TRAF and TNF receptor associated protein
, TRAF and TNF receptor-associated protein
, VPg unlinkase
, tyr-DNA phosphodiesterase 2
, tyrosyl-RNA phosphodiesterase
, TRAF and TNF receptor-associated protein homolog
, Tyr-DNA phosphodiesterase 2
, Traf and Tnf receptor associated protein
, immune transcriptional repressor
, traf and tnf receptor associated protein, like
, tyrosyl-DNA phosphodiesterase 2