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Brm-HDAC3-Erm repressor complex suppresses dedifferentiation of intermediate neural progenitors back into type II neuroblasts.
Hdac3 served as an important regulator of the PI3K pathway and revealed a novel link between histone acetylation and growth control.
Overexpressing any of HDAC 3, 6, or 11 suppresses CGG repeat-induced neurodegeneration in a Drosophila model of fragile X (show FMR1 ELISA Kits) tremor ataxia (show USP14 ELISA Kits) syndrome.
) DHDAC1 (show HDAC1 ELISA Kits) and -3 have distinct functions in the control of gene expression
Mutant larvae display small imaginal discs, which result from abnormally elevated levels of apoptosis. This cell death occurs as a cell-autonomous response to HDAC3 loss and is accompanied by increased expression of the pro-apoptotic gene, hid.
HDAC3 upregulation is associated with hepatocellular carcinoma.
High HDAC3 expression is associated with pancreatic cancer.
These findings pinpoint that TGF-beta (show TGFB1 ELISA Kits) represses miR (show MLXIP ELISA Kits)-30d through a Smad2 (show SMAD2 ELISA Kits)/3-HDAC3-NCoR (show NCOR1 ELISA Kits) repression complex and provide novel insights into a potential target for the treatment of podocyte injury-associated glomerulopathies.
Results show the direct regulation of CAGE expression by HDAC3 and that HDAC3-CAGE axis regulates the activation of EGFR (show EGFR ELISA Kits). HDAC3 targets CAGE to regulate the tumorigenic potential and angiogenic potential of cancer cells.
HDAC3 knockdown or HDAC3 inhibition was associated with simultaneous upregulation of the expression of miR130a and downregulation of the expression of TNF1alpha in peripheral blood mononuclear cells.
Data suggest that complexes of HDAC3-H1.3 with NCOR1 and NCOR2/SMRT accumulate on chromatin in synchronized HeLa cells in late G2 phase and mitosis; deacetylation activity of HDAC3 is activated via phosphorylation of Ser-424 by CK2 only in mitosis.
this is the first report on the regulation mechanism of SIRT7 (show SIRT7 ELISA Kits) gene, in which, HDAC3 collaborated with C/EBPalpha (show CEBPA ELISA Kits) to occupy its responding element in the upstream region of SIRT7 (show SIRT7 ELISA Kits) gene and repressed its expression in human cells.
Among the class II HDACs, HDAC4 (show HDAC4 ELISA Kits) interacted with both MR and HDAC3 after aldosterone stimulation. The nuclear translocation of HDAC4 (show HDAC4 ELISA Kits) was mediated by protein kinase A (PKA) and protein phosphatases (PP)
miR (show MLXIP ELISA Kits)-335 exerted apoptotic effects and inhibited ubiquitination of HDAC3 in anti-cancer drug-resistant cancer cell lines. miR (show MLXIP ELISA Kits)-335 negatively regulated the invasion, migration, and growth rate of cancer cells.
ZBP-89 (show ZNF148 ELISA Kits) attenuates HDAC3 by increasing IkappaB degradation, dependent on Pin1 (show PIN1 ELISA Kits) but independent of NF-Kappab (show NFKB1 ELISA Kits)
Hdac3 induces an medullary thymic epithelial cells-specific transcriptional program.
concurrent declines in transcription and phosphorylation combine to suppress Hdac3 activity in aging bone, and reduced Hdac3 activity in osteochondroprogenitor cells contributes to increased marrow adiposity associated with aging.
HDAC3 is required for efficient activation of E-box-driven gene expression, blocks CRY1 (show CRY1 ELISA Kits) degradation and promotes BMAL1 (show ARNTL ELISA Kits) and CRY1 (show CRY1 ELISA Kits) association.
GC-induced direct repression, but not bindings of GR and of corepressors NCoR1 (show NCOR1 ELISA Kits)/SMRT, was abolished, indicating that HDAC3 is instrumental in IR nGRE-mediated repression
GR SUMOylation site is mandatory for the formation of a GR-small ubiquitin-related modifiers (SUMOs)-SMRT/NCoR1 (show NCOR1 ELISA Kits)-HDAC3 repressing complex, which is indispensable for NF-kappaB (show NFKB1 ELISA Kits)/AP1 (show JUN ELISA Kits)-mediated GC-induced tethered indirect transrepression in vitro
studies reveal an intricate epigenetic pathway where Hdac3 is required to repress miR-17-92 expression to allow for proper TGF-beta (show TGFB1 ELISA Kits) signaling during lung sacculation
Bach2 is suggested to cooperate with HDAC3-containing co-repressor complexes in B cells to regulate the stage-specific expression of Prdm1 (show PRDM1 ELISA Kits) by writing epigenetic modifications at the Prdm1 (show PRDM1 ELISA Kits) locus.
Hdac3 cooperates with p300 (show NOTCH1 ELISA Kits) to prime and maintain oligodendrocyte identity
Wild-type HDAC3 or catalytically inactive HDAC3 expression rescues aberrant endothelial-to-mesenchymal transition and epigenetic silencing of Tgf-beta1 (show TGFB1 ELISA Kits) in HDAC3-null outflow tracts and semilunar valves.
Study shows that conditional deletion of an epigenetic regulator, Hdac3, in osteoblast progenitor cells abrogates high fat diet-induced insulin (show INS ELISA Kits) resistance and hepatic steatosis. These Hdac3-deficient mice have reduced bone formation and lower circulating levels of total and undercarboxylated osteocalcin (show BGLAP ELISA Kits), coupled with decreased bone resorption activity.
These results revealed a novel and specific role of hdac3 in liver development and the distinct functions between hdac1 (show HDAC1 ELISA Kits) and hdac3 in zebrafish embryonic development.
Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family. It has histone deacetylase activity and represses transcription when tethered to a promoter. It may participate in the regulation of transcription through its binding with the zinc-finger transcription factor YY1. This protein can also down-regulate p53 function and thus modulate cell growth and apoptosis. This gene is regarded as a potential tumor suppressor gene.
, histone Deacetylase-3
, histone deacetylase 3
, HDAC3 splicing HDAC3alpha
, HDAC3 splicing HDAC3beta
, HDAC3 splicing HDAC3delta
, HDAC3 splicing HDAC3gamma
, histone deacetylase-3