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Human HDAC3 Protein expressed in Baculovirus infected Insect Cells - ABIN2004315
Pajerowski, Nguyen, Aghajanian, Shapiro, Shapiro: NKAP is a transcriptional repressor of notch signaling and is required for T cell development. in Immunity 2009
Show all 4 references for ABIN2004315
Human HDAC3 Protein expressed in Wheat germ - ABIN1306448
Jiang, Ye, Guo, Lu, Gao: Inhibition of HDAC3 promotes ligand-independent PPAR? activation by protein acetylation. in Journal of molecular endocrinology 2014
Brm (show SMARCA2 Proteins)-HDAC3-Erm (show MSN Proteins) 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 Proteins) tremor ataxia (show USP14 Proteins) syndrome.
) DHDAC1 (show HDAC1 Proteins) 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.
Histone deacetylase 3 regulates the inflammatory gene expression programme of rheumatoid arthritis fibroblast-like synoviocytes.
Study demonstrated an association of elevated HDAC3 activity and HDAC3 mRNA expression in patients with type 2 diabetes (T2DM) which was positively correlated with proinflammation and insulin (show INS Proteins) resistance.
HDAC3 upregulation is associated with hepatocellular carcinoma.
High HDAC3 expression is associated with pancreatic cancer.
These findings pinpoint that TGF-beta (show TGFB1 Proteins) represses miR (show MLXIP Proteins)-30d through a Smad2 (show SMAD2 Proteins)/3-HDAC3-NCoR (show NCOR1 Proteins) 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 Proteins). 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 Proteins) gene, in which, HDAC3 collaborated with C/EBPalpha (show CEBPA Proteins) to occupy its responding element in the upstream region of SIRT7 (show SIRT7 Proteins) gene and repressed its expression in human cells.
Among the class II HDACs, HDAC4 (show HDAC4 Proteins) interacted with both MR and HDAC3 after aldosterone stimulation. The nuclear translocation of HDAC4 (show HDAC4 Proteins) was mediated by protein kinase A (PKA) and protein phosphatases (PP)
These results demonstrate that HDAC3 and SCAP control symbiotic pathways of liver lipid metabolism that are critical for suppression of lipotoxicity.
The study describes an interaction network of STAT5a (show STAT5A Proteins)/LSD1 (show KDM1A Proteins)/HDAC3 and a dual function of LSD1 (show KDM1A Proteins)/HDAC3 on STAT5a (show STAT5A Proteins)-dependent transcription, defined by protein-protein interactions, genomic binding localization/affinity and motifs.
Both the acetylation and SUMOylation status of the PXR protein is affected by its ability to associate with the lysine de-acetylating enzyme HDAC3 in a complex with SMRT.
The present study provides the first critical in vivo evidence showing a causal link between epigenetic modification of miR (show MLXIP Proteins)-10a mediated by HDAC3 and the development of diabetic nephropathy, and these results elucidate that HDAC3/miR (show MLXIP Proteins)-10a/CREB1 (show CREB1 Proteins) serves as a new mechanism underlying kidney injury, providing potential therapeutic targets in type 2 diabetes
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 Proteins) degradation and promotes BMAL1 (show ARNTL Proteins) and CRY1 (show CRY1 Proteins) association.
GC-induced direct repression, but not bindings of GR and of corepressors NCoR1 (show NCOR1 Proteins)/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 Proteins)-HDAC3 repressing complex, which is indispensable for NF-kappaB (show NFKB1 Proteins)/AP1 (show JUN Proteins)-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 Proteins) signaling during lung sacculation
These results revealed a novel and specific role of hdac3 in liver development and the distinct functions between hdac1 (show HDAC1 Proteins) 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