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Human Polyclonal DAXX Primary Antibody for ICC, IF - ABIN4304326
Stepp, Meyers, McBride: Sp100 provides intrinsic immunity against human papillomavirus infection. in mBio 2013
Show all 8 Pubmed References
Human Monoclonal DAXX Primary Antibody for IHC (fro), WB - ABIN2473232
Barnes: Toxicity equivalents and EPA's risk assessment of 2,3,7,8-TCDD. in The Science of the total environment 1991
Show all 4 Pubmed References
Human Polyclonal DAXX Primary Antibody for IHC (p), WB - ABIN537598
Cantrell, Bresnahan: Interaction between the human cytomegalovirus UL82 gene product (pp71) and hDaxx regulates immediate-early gene expression and viral replication. in Journal of virology 2005
Show all 3 Pubmed References
Human Monoclonal DAXX Primary Antibody for FACS, IF - ABIN965974
Yang, Khosravi-Far, Chang, Baltimore: Daxx, a novel Fas-binding protein that activates JNK and apoptosis. in Cell 1997
Show all 3 Pubmed References
Human Polyclonal DAXX Primary Antibody for ICC, IF - ABIN315683
Weisbrod, Zhang, Jain, Barak, Quezado, Kebebew: Altered PTEN, ATRX, CHGA, CHGB, and TP53 expression are associated with aggressive VHL-associated pancreatic neuroendocrine tumors. in Hormones & cancer 2013
Human Monoclonal DAXX Primary Antibody for ICC, IP - ABIN302079
Símová, Klíma, Cermak, Sourková, Andera: Arf and Rho GAP adapter protein ARAP1 participates in the mobilization of TRAIL-R1/DR4 to the plasma membrane. in Apoptosis : an international journal on programmed cell death 2008
Show all 5 Pubmed References
Human Monoclonal DAXX Primary Antibody for ICC, WB - ABIN94302
Leal-Sanchez, Couzinet, Rossin, Abdel-Sater, Chakrabandhu, Luci, Anjuere, Stebe, Hancock, Hueber: Requirement for Daxx in mature T-cell proliferation and activation. in Cell death and differentiation 2007
Cow (Bovine) Polyclonal DAXX Primary Antibody for IHC, IHC (p) - ABIN4304321
Yang, Hu, Chen, Zhu, Li, Lu, Li, Dong: Necrostatin-1 protects hippocampal neurons against ischemia/reperfusion injury via the RIP3/DAXX signaling pathway in rats. in Neuroscience letters 2017
ATRX, DAXX or MEN1 mutant pancreatic neuroendocrine tumors are a distinct alpha-cell signature subgroup
Data show that phosphatase and tensin homolog (PTEN) interacts with death domain associated protein (DAXX) and, in turn PTEN directly regulates oncogene expression by modulating DAXX-histone H3.3 (H3.3) association on the chromatin.
Daxx directly binds to the DNA-binding domain of Slug, impeding histone deacetylase 1 (HDAC1) recruitment and antagonizing Slug E-box binding. This, in turn, stimulates E-cadherin and occludin expression and suppresses Slug-mediated epithelial-mesenchymal transition (EMT) and cell invasiveness.
Results show that the X-linked nuclear protein (ATRX)-Fas death domain-associated protein (DAXX) complex is involved in gene repression and telomere chromatin structure.
disruption of CENP-B/Daxx-dependent H3.3 pathway deregulates heterochromatin marks H3K9me3, ATRX and HP1alpha at centromeres and elevates chromosome instability
Disrupting the ATRX/DAXX complex and inhibiting telomerase activity in telomerase-positive cancer cells lead to the alternative lengthening of telomeres switch.
Study found that enhanced nuclear accumulation of Daxx correlated with the malignant phenotype in gastric mucosa.
ATRX or DAXX loss was proved to be an independent predictor for OS of PanNETs in a multivariate Cox regression analysis including well-established risk factors; tumor stage and tumor grade.
Both primary Alternative lengthening of telomeres(ALT) -positive and ATRX/DAXX-negative PanNETs are independently associated with aggressive clinicopathologic behavior and displayed reduced recurrence-free survival. In contrast, ALT activation and loss of ATRX/DAXX are both associated with better overall survival in patients with metastases
Whole-exome sequencing has identified recurrent mutations in the genes DAXX and ATRX, which correlate with loss of protein expression and alternative lengthening of telomeres (ALT).ALT and DAXX/ATRX loss in PanNETs was associated with shorter disease-free survival (DFS) and disease-specific survival (DSS) and likely plays a significant role in driving metastatic disease
We propose that mutations in alpha thalassemia-mental retardation syndrome X-linked (ATRX)/death-domain associated protein (DAXX) prime alternative lengthening of telomeres activation by disrupting telomeric heterochromatin.
Structural and biochemical characterization of DAXX-ATRX interaction.
Structural basis for DAXX interaction with ATRX.
Given the high frequency of ATRX and DAXX mutations in cancer, these chromatin regulators likely play a key role in pathogenesis [review]
H3.Y discriminates between HIRA and DAXX chaperone complexes and reveals unexpected insights into human DAXX-H3.3-H4 binding and deposition requirements.
DAXX gene plays a role in the pathogenesis of neuroendocrine pancreatic neoplasms.
The widespread dynamic nature of DAXX methylation in association with trophoblast differentiation and placenta-associated pathologies is consistent with an important role for this gene in proper placental development and function.
findings reveal a previously unappreciated cross-talk between two crucial tumor suppressor genes, MEN1 and DAXX, thought to work by independent pathways
The interaction of Daxx C-terminal domain and androgen receptor suppresses cholesterol synthesis.Daxx C-terminal domain binds directly to androgen receptor.
HDAC1 and DAXX are co-repressors associated with epigenetic regulation that help to control promoter histone acetylation reactions involved in regulating GAD67.
DAXX can induce ovarian cancer ascites formation by activating the ERK signal pathway and binding to CEBP-beta.
PML protein organizes heterochromatin domains where it regulates histone H3.3 deposition by ATRX and DAXX.
data support a model in which activation of myogenic differentiation results in PML NB loss, chromatin reorganization and DAXX relocalization, and provides a paradigm for understanding the consequence of PML loss in other cellular contexts, such as during cancer development and progression
This study provides important details regarding the expression and post-translational modifications of DAXX in aging in the entire organism and provides reference data for the deregulation observed in age-associated diseases.
This is a promising novel therapeutic approach because it appears to be effective in a model producing severe injury by interfering with an array of proximal signals and effectors of the ischemic cascade, upstream of JNK, caspases, and BIM and BAX activation.
Daxx and Atrx safeguard the genome by silencing repetitive elements when DNA methylation levels are low.
The protein levels of Daxx is reduced in Stella-null oocytes and embryos.
Daxx selectively represses IL-6 transcription through HDAC1-mediated histone deacetylation
Overall, these data imply a regulatory role for Daxx in reovirus-induced apoptosis, depending on its location in the nucleus or cytoplasm.
phosphorylation of Daxx by RIP3 comprises an important part of ischemic necrosis in rat retinal ganglion cells
DAXX is associated with regulatory regions of selected activity-regulated genes, where it promotes H3.3 loading upon membrane depolarization. DAXX loss not only affects H3.3 deposition but also impairs transcriptional induction of these genes.
Daxx, a HIPK kinase substrate in the apoptosis pathway, was phosphorylated by HIPK3 at Ser-669 in response to cAMP stimulation.
Neither Daxx nor PML, the main players of ND10-based immunity, are required for the block to viral gene expression in the S/G2 phase.
HIRA interacts with H3.3/H4 in the absence of Daxx.
Both Daxx and macrophage Ste20-like kinase (MST)1 are key mediators of microglial cell death induced by the proinflammatory cytokine interferon (IFN)-gamma.
Characterizing the N- and C-terminal Small ubiquitin-like modifier (SUMO)-interacting motifs of the scaffold protein DAXX.
Using the transcriptional coregulator Daxx as a model, we show that SUMO paralog-selective binding and conjugation are regulated by phosphorylation of the Daxx SUMO-interacting motif (SIM).
suppresses gp130-mediated cell growth and survival by two independent mechanisms: inhibition of STAT3-induced transcription and down-regulation of Bcl2 expression
Daxx functions as an H3.3-specific chaperone and facilitates the deposition of H3.3 at heterochromatin loci in the context of the ATRX-Daxx complex
Overexpressed WT human DJ-1 prevents Daxx translocation and abolishes cytotoxicity in mouse Neuro-2a cells.
Daxx mRNA was detected in embryonic development from 6 h to 120 h and in all 11 selected zebrafish tissues, and Daxx expression first increased and then decreased during megalocytivirus infectious spleen and kidney necrosis virus infection.
This gene encodes a multifunctional protein that resides in multiple locations in the nucleus and in the cytoplasm. It interacts with a wide variety of proteins, such as apoptosis antigen Fas, centromere protein C, and transcription factor erythroblastosis virus E26 oncogene homolog 1. In the nucleus, the encoded protein functions as a potent transcription repressor that binds to sumoylated transcription factors. Its repression can be relieved by the sequestration of this protein into promyelocytic leukemia nuclear bodies or nucleoli. This protein also associates with centromeres in G2 phase. In the cytoplasm, the encoded protein may function to regulate apoptosis. The subcellular localization and function of this protein are modulated by post-translational modifications, including sumoylation, phosphorylation and polyubiquitination. Alternative splicing results in multiple transcript variants.
CENP-C binding protein
, ETS1-associated protein 1
, Fas-binding protein
, death domain-associated protein 6
, death-associated protein 6
, fas death domain-associated protein
, death-domain associated protein
, death associated protein 3
, Fas death domain-associated protein
, LOW QUALITY PROTEIN: death domain-associated protein 6
, death-associated protein 6 L homeolog