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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 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 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
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
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
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 (show AR Antibodies) suppresses cholesterol synthesis.Daxx C-terminal domain binds directly to androgen receptor (show AR Antibodies).
HDAC1 (show HDAC1 Antibodies) and DAXX are co-repressors associated with epigenetic regulation that help to control promoter histone acetylation reactions involved in regulating GAD67 (show GAD1 Antibodies).
We provide an overview of the individual components (ATRX, DAXX and/or H3.3) tested in each study and propose a model where the ATRX/DAXX chaperone complex deposits H3.3 to maintain the H3K9me3 modification at heterochromatin throughout the genome.
Daxx and Atrx (show ATRX Antibodies) safeguard the genome by silencing repetitive elements when DNA methylation (show HELLS Antibodies) levels are low.
Studies of the dynamics of the response of PML (show PML Antibodies) nuclear body components and IFI16 (show IFI16 Antibodies) to invading herpes simplex virus 1 genomes demonstrated that human Daxx (hDaxx) and IFI16 (show IFI16 Antibodies) respond more rapidly than PML (show PML Antibodies).
identifying Daxx as a broad cellular inhibitor of reverse-transcription. Altogether, these findings unravel a novel antiviral function for PML (show PML Antibodies) and PML (show PML Antibodies) nuclear body-associated protein Daxx
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 (show MAPK8 Antibodies), caspases, and BIM (show BCL2L11 Antibodies) and BAX (show BAX Antibodies) activation.
The protein levels of Daxx is reduced in Stella (show DPPA3 Antibodies)-null oocytes and embryos.
Daxx selectively represses IL-6 (show IL6 Antibodies) transcription through HDAC1 (show HDAC1 Antibodies)-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 (show MPRIP Antibodies) 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 (show HIPK3 Antibodies) at Ser (show SIGLEC1 Antibodies)-669 in response to cAMP stimulation.
Neither Daxx nor PML (show PML Antibodies), the main players of ND10-based immunity, are required for the block to viral gene expression in the S/G2 (show STRN3 Antibodies) phase.
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.
28S ribosomal protein S29, mitochondrial
, death associated protein 3
, 28S ribosomal protein S29, mitochondrial-like
, 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
, Fas death domain-associated protein
, death-domain associated protein