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Human HDAC2 Protein expressed in Hi-5 - ABIN667944
Taunton, Hassig, Schreiber: A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. in Science (New York, N.Y.) 1996
Show all 2 references for ABIN667944
The results imply that HDAC2 is involved in the transcriptional regulation of human odontoblasts in vivo.
Endothelial-Mesenchymal Transition is initiated by recruitment of aberrantly phosphorylated DNMT1 (show DNMT1 Proteins) to the RASAL1 (show RASAL1 Proteins) CpG island promoter by HDAC2, causing aberrant promoter methylation and transcriptional suppression.
Selective inhibition of HDAC2 in lung tumor cell causes survivin (show BIRC5 Proteins) downregulation through activation of p53 (show TP53 Proteins), which is mediated by downregulation of Mdm2 (show MDM2 Proteins).
our study revealed that HDAC2 is overexpressed in colorectal cancer (CRC (show CALR Proteins)) cells; its knockdown can increase the sensitivity of CRC (show CALR Proteins) cells to doxorubicin via upregulation of ABCB1 (show ABCB1 Proteins)
Pancreatic adenocarcinoma patients with enhanced HDAC-1 (show HDAC1 Proteins) and -6 expression showed significantly longer survival times compared to those with low expression, while a borderline association concerning HDAC-2 expression was noted.
Lymphocyte senescence in COPD (show ARCN1 Proteins) is associated with loss of HDAC2 in CD28nullCD8+ T and NKT (show SLC22A6 Proteins)-like cells.
Results show that mRNA expression of histone deacetylases HDAC1 (show HDAC1 Proteins) and HDAC2 were significantly increased in peripheral blood mononuclear cells of patients with with Graves' disease compared to controls.
HDAC2 may not confer susceptibility to Schizophrenia in Han Chinese.
In endothelial dysfunction, HDAC2 levels were reciprocally regulated by ectopic expression of NEDD8 (show NEDD8 Proteins) and the de-NEDDylating enzyme SENP8 (show SENP8 Proteins).
shRNA-mediated knockdown of HDAC1 (show HDAC1 Proteins) or HDAC2 resulted in growth inhibition of B-cell acute lymphoblastic leukemia cells.
HDAC2 may regulate the expression of immediate early (show JUN Proteins) genes, in part, by prolonging the actions of pCREB in the mouse nucleus accumbens.
Injecting these oocytes with Hdac2 partially restores DNMT3A2 (show DNMT3A Proteins) nuclear staining.
Our data show that: i) HDAC2 levels and activity are increased in NPC (show NPC1 Proteins) neuronal models and in Npc1 (show NPC1 Proteins)(-/-) mice; ii) inhibition of c-Abl (show ABL1 Proteins) or c-Abl (show ABL1 Proteins) deficiency prevents the increase of HDAC2 protein levels and activity in NPC (show NPC1 Proteins) neuronal models
This study reveals a dominant negative effect of catalytically inactive HDAC2 on specific corepressor complexes resulting in histone hyperacetylation, transcriptional derepression, and, ultimately, perinatal lethality.
This study demonstrated that hdac2 increase in skeletal muscle in muscle atrophy.
Intestinal epithelial cell (IEC) determination and intestinal homeostasis are highly dependent on Hdac1 (show HDAC1 Proteins) and Hdac2 activity levels, and changes in the IEC acetylome may alter the mucosal environment.
results demonstrate that combined HDAC1 (show HDAC1 Proteins) and HDAC2 ablation promotes survival of axotomized retinal ganglion cells; HDAC1 (show HDAC1 Proteins)/2 ablation inhibited the apoptotic pathway by impairing acetylation status of p53 (show TP53 Proteins) and reducing PUMA (show BBC3 Proteins) expression, thereby contributing to the ensuing enhanced neuroprotection due to HDAC1 (show HDAC1 Proteins)/2 depletion
Scopolamine induced memory impairment along with increased gene expression of HDAC2 in corpus striatum.
mechanistic evidence for the gene-specific transcription repression activity of Tet2 via histone deacetylation and for the prevention of constant transcription activation at the chromatin level for resolving inflammation
HDAC2 might be a downstream effector of Jak2 (show JAK2 Proteins) to mediate cardiac hypertrophic response by pressure overload or Ang-II (show AGT Proteins).
This gene product belongs to the histone deacetylase family. Histone deacetylases act via the formation of large multiprotein complexes, and are responsible for the deacetylation of lysine residues at the N-terminal regions of core histones (H2A, H2B, H3 and H4). This protein forms transcriptional repressor complexes by associating with many different proteins, including YY1, a mammalian zinc-finger transcription factor. Thus, it plays an important role in transcriptional regulation, cell cycle progression and developmental events. Alternative splicing results in multiple transcript variants.
YY1-associated factor 1
, transcriptional regulator homolog RPD3
, YY1 transcription factor-binding protein
, histone deacetylase-2