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findings implicate TOP2A cleavage as a broad DNA damage mechanism in oncogenic translocations as well as a functional role of TOP2A cleavage in regulating transcription elongation and gene activation.
TOP2A acts as a co-activator of beta-catenin (show CTNNB1 Proteins) and activates Epithelial-mesenchymal transition process.
ProEx C is an immunohistochemical cocktail containing antibodies direct against topoisomerase IIalpha (TOP2A) and minichromosome maintenance 2 (MCM2 (show MCM2 Proteins)) proteins. This brief review covers the effective utility of ProEx C as adjunct tool in assessing the urothelial lesions in urine cytology, also providing prognostic and therapeutic information to help in clinical decisions.
High TOP2A expression was significantly associated with longer time to progression after EDP-M. TOP2A and TS proteins assessed by immunohistochemistry significantly correlated with mRNA expression. Immunohistochemical TOP2A expression was associated with a non-significant better response and longer TTP (show ADAMTS13 Proteins) after EDP-M.
Data show that comparing with Ki-67 (show MKI67 Proteins) and TOP2A, RacGAP1 (show RACGAP1 Proteins) allowed for a clearer prognostic statement.
These findings reveal a novel, p53 (show TP53 Proteins)-independent activity of Mdm2 (show MDM2 Proteins) and have important implications for the choice of chemotherapeutic agents in the treatment of Mdm2 (show MDM2 Proteins)-overexpressing tumors. Herein is shown that tumor cells with MDM2 (show MDM2 Proteins) amplification are selectively resistant to treatment with topoisomerase II (show TOP2 Proteins) poisons but not other DNA damaging agents
The methodology is useful for a high-throughput analysis of drugs that poison Top2, allowing not just the discrimination of the Top2 isoform that is targeted but also to track its removal
TOP2A was identified in association with the progression and prognosis of pancreatic ductal adenocarcinoma probably by regulating cell cycle and p53 (show TP53 Proteins) signaling pathway.
the relation between TOP2A levels and sensitivity for doxorubicin was examined, confirming reports that TOP2A mRNA levels were overexpressed in MPNST and showing that MPNST cell lines exhibited relatively high TOP2A protein levels and sensitivity to doxorubicin.
The decatenation checkpoint is regulated, not only by topo IIalpha, as previously reported, but also by topo IIbeta. The decatenation checkpoint is most efficient when both isoforms are present. Deletion of most of the C-terminus of topo IIalpha, while preserving the nuclear localization signal (NLS (show ALDH1A2 Proteins)), enhances the decatenation checkpoint and sensitivity to topo II (show TOP2 Proteins)-targeted drugs. Mutation of Y640 in topo IIalpha inhibi...
Polyamide functionalisation at the N1-position offers a design strategy to improve drug-like properties. Dicationic HxIP* 3 increased topo IIalpha expression and chemosensitivity to topo II (show TOP2 Proteins)-targeting agents.
TOP2 (show TOP2 Proteins) and BAF (show BANF1 Proteins) cooperate to recruit pluripotency factors, which explains some of the instructive roles of BAF (show BANF1 Proteins) complexes.
Deletion or deficiency of PTEN leads to down regulation of TOP2A, dysfunction of the decatenation checkpoint and incomplete DNA decatenation in G2 and M phases.
Inhibition of DNA topoisomerase II (show TOP2 Proteins) selectively reduces the threat of tumorigenicity
Cohesin removal is a prerequisite for the posterior topoisomerase IIalpha-mediated resolution of persisting catenations between segregating chromatids during anaphase II.
Data show that unfolded protein response (UPR)-induced changes in topoisomerase IIalpha (Topo IIalpha) protein levels are not responsible for resistance to etoposide, and that the PERK plays a Topo IIalpha-independent role in altered sensitivity to the drug.
Topoisomerase IIa not only contributes to stem-cell transcriptome regulation but also primes developmental genes for subsequent activation upon differentiation.
studies indicate that the ability of TOP2A to prevent DNA entanglement at mitosis requires BAF (show BANF1 Proteins) complexes and suggest that this activity contributes to the role of BAF (show BANF1 Proteins) subunits as tumour suppressors
our data reveal TDP2 (show TDP2 Proteins)-mediated error-free NHEJ as an efficient and accurate mechanism to repair TOP2 (show TOP2 Proteins)-induced DSBs
DNA topoisomerase II (show TOP2 Proteins) distribution in mouse preimplantation embryos
This gene encodes a DNA topoisomerase, an enzyme that controls and alters the topologic states of DNA during transcription. This nuclear enzyme is involved in processes such as chromosome condensation, chromatid separation, and the relief of torsional stress that occurs during DNA transcription and replication. It catalyzes the transient breaking and rejoining of two strands of duplex DNA which allows the strands to pass through one another, thus altering the topology of DNA. Two forms of this enzyme exist as likely products of a gene duplication event. The gene encoding this form, alpha, is localized to chromosome 17 and the beta gene is localized to chromosome 3. The gene encoding this enzyme functions as the target for several anticancer agents and a variety of mutations in this gene have been associated with the development of drug resistance. Reduced activity of this enzyme may also play a role in ataxia-telangiectasia.
, DNA topoisomerase (ATP-hydrolyzing)
, DNA topoisomerase 2-alpha
, DNA topoisomerase II, 170 kD
, DNA topoisomerase II, alpha isozyme
, DNA Topoisomerase II alpha
, topoisomerase (DNA) 2 alpha
, DNA topoisomeraseII_alpha
, topoisomerase (DNA) II alpha
, Thimet metalloendopeptidase 2
, Zincin-like metalloproteases family protein 2