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anti-Human Topoisomerase II alpha Antibodies:
anti-Mouse (Murine) Topoisomerase II alpha Antibodies:
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Human Polyclonal Topoisomerase II alpha Primary Antibody for ICC, IF - ABIN4361369
Lindén, Segersten, Runeson, Wester, Busch, Pettersson, Lind, Malmström: Tumour expression of bladder cancer-associated urinary proteins. in BJU international 2013
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Human Monoclonal Topoisomerase II alpha Primary Antibody for IHC (p), WB - ABIN2734025
Jiang, Mohan, Endo, Shen, Wu: Type IIB DNA topoisomerase is downregulated by trastuzumab and doxorubicin to synergize cardiotoxicity. in Oncotarget 2018
Arabidopsis thaliana Polyclonal Topoisomerase II alpha Primary Antibody for IL, WB - ABIN334538
Xie, Lam: Abundance of nuclear DNA topoisomerase II is correlated with proliferation in Arabidopsis thaliana. in Nucleic acids research 1995
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Human Monoclonal Topoisomerase II alpha Primary Antibody for IF, IHC (p) - ABIN563224
Poonperm, Takata, Hamano, Matsuda, Uchiyama, Hiraoka, Fukui: Chromosome Scaffold is a Double-Stranded Assembly of Scaffold Proteins. in Scientific reports 2015
TOP2A was overexpressed in bladder urothelial carcinoma (BLCA) and could serve as a prognostic biomarker for BLCA. Moreover, TOP2A is functionally important for the proliferation, invasion and survival of BLCA cells.
Interaction network analysis of YBX1 for identification of therapeutic targets in adenocarcinomas found 12 genes playing important roles in the network formation; among them, two genes FOXM1 and TOP2A were found to be in central network formation, which makes them a common target for therapeutics.
The expression of TOP2A in colon cancer tissues was increased compared to normal adjacent tissues. The proliferation and invasion of colon cancer cells can be suppressed in colon cancer cells by depleting of TOP2A. TOP2A may serve as an oncogene in colon cancer.
We demonstrate that Topo2a is SUMOylated in an ICRF193-dependent manner by NSE2 at a novel non-canonical site (K1520) and that K1520 sumoylation is required for chromosome segregation but not the G2 arrest.
acetylation of specific sites involved in the allosteric regulation of human Top2 may provide a mechanism for modulation of its catalytic activity.
Study have demonstrated that high expression rates of proliferative markers TOP2A and MCM6 in colorectal cancer is linked to a beneficial patient outcome. According to the general opinion, a high expression rate correlates with a poor patient outcome and study was able to refute this assertion.
nuclear division cycle 80, cyclin B2 and topoisomerase 2alpha may serve important roles in adrenocortical tumor development.
We report here that both known type II topoisomerases Top2a and Top2b are present in mammalian mitochondria, with especially Top2b regulating the supercoiling state of mtDNA. Loss of Top2b or its inhibition by ciprofloxacin results in accumulation of positively supercoiled mtDNA, followed by cessation of mitochondrial transcription and replication initiation, causing depletion of mtDNA copy number.
SENP3 phosphorylation decreased its interaction with Topo II alpha, resulting in reduced SENP3 deSUMOylation activity on Topo II alpha. Furthermore, we observed mitotic arrest, increased chromosome instability, and promotion of tumorigenesis in cells expressing a nonphosphorylatable SENP3 mutant
DNA topoisomerase II alpha (TOP2A) is associated with a longer time to progression (TTP) following pegylated liposomal doxorubicin (PLD)-treatment. Patients with TOP2A expression treated with PLD monotherapy achieved a longer TTP compared with PLD-doublet therapy. TOP2A status might predict activity of PLD in patients with platinum resistant or partially platinum-sensitive epithelial ovarian cancer.
no significant association between, MAPK and topoIIalpha expression and overall survival in ovarian serous carcinomas
The topoisomerase II alpha expression correlated more with invasiveness than with extensiveness, which might make it an eminently useful marker in the assessment of aggressive pituitary adenoma behaviour.
TOP2A gene alterations and CEP17 polysomy may have prognostic and predictive role in TNBC treated with adjuvant Anthracyclines.
TOP2A is highly expressed in liver cancer tissues and acts as an oncogene.
USP15 is required for TOP2A accumulation, and USP15 depletion leads to the formation of anaphase chromosome bridges.
We identified 16 potentially druggable candidates. Among them, NEK2, BIRC5, and TOP2A were also found to be amplified in breast cancer, suggesting that they could act as strategic players in the obese-deregulated transcriptome.
Spearman's rank correlation analysis and Bonferroni correction were used to compare the values of DKI and the expression levels of GFAP, Topo IIalpha, and MGMT between the 2 groups.
Alternative processing of TOP2alpha pre-mRNA, and subsequent synthesis of TOP2alpha/90, may be an important mechanism regulating the formation and/or stability of cytotoxic TOP2alpha/170-DNA covalent complexes in response to TOP2alpha-targeting agents
Study found both high TOP2A mRNA expression and protein expression in HCMV-infected glioma cells. High TOP2A expression in GBM was correlated with cell proliferation and malignant transformation in HCMV-positive glioma cells. Also TOP2A was identified as a direct target gene of miR-144.
A tri-serine cluster within the topoisomerase IIalpha-interaction domain of the BLM helicase is required for regulating chromosome breakage in human cells.
RNF168 interacts with TOP2alpha to mediate its polyubiquitylation and RNF168 deficiency confers resistance to ICRF-193, a TOP2 catalytic inhibitor, and cytotoxic anti-cancer drug etoposide in cultured mouse cells.
Topo IIalpha plays an important role in adipogenesis.
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-targeting agents.
TOP2 and BAF cooperate to recruit pluripotency factors, which explains some of the instructive roles of BAF 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 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 complexes and suggest that this activity contributes to the role of BAF subunits as tumour suppressors
our data reveal TDP2-mediated error-free NHEJ as an efficient and accurate mechanism to repair TOP2-induced DSBs
Top2alpha is suggested to be a universal target for cancer immunotherapy.
DNA topoisomerase II distribution in mouse preimplantation embryos
DNA topoisomerase II is essential for preimplantation mouse development
The role of topoisomerase II in the excision of DNA loop domains during apoptosis.
CCAAT binding factor (CBF) binding mediates cell cycle activation of this enzyme; conventional CBF activation domains are not required.
Gly881, which is located in the ATP binding site, was replaced by Arg in DNA topoisomerase IIalpha of NC-190-resistance tumor cells. These cells were also etoposide-resistant.
Results suggest that topo IIalpha-depleted cells with the droplet-like nuclear structure induce apoptosis, which is dependent on caspase and p53 activity during the G1 phase in mammalian cells.
The functional status of pRb protein may influence sensitivity to etoposide by facilitating the repair of trapped TOP2-DNA complexes.
Expression of the topoisomerase IIalpha gene in confluent NIH 3T3 cells was induced by treatment with f-PIP
role in maintaining the proper level and dynamics of proteome oxidation during effector-triggered immunity
Interacts with protein targets to mediate salicylic acid (SA)-dependent signaling necessary for the immune response to avirulent pathogens.
The absence of zygotic top2a is not fully compensated for by maternal, zygotic or ectopic top2b mRNA suggesting distinct functions of Top2a and Top2b in embryonic development.
Results confirm a conserved role for topoisomerase II alpha (TOP2A) in vertebrates as well as a dose-sensitive requirement for top2a in adults.
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
, topoisomerase 2