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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 current findings implicate the HDAC2/miR (show MLXIP Proteins)-101/AMPK (show PRKAA1 Proteins) pathway as a critical mediator of AD pathogenesis. These studies also highlight the importance of epigenetics in AD and provide novel therapeutic targets.
Increased cancer-specific mortality was significantly associated with HDAC2 expression, mortality was also increased with high HDAC1 (show HDAC1 Proteins) expression.
HDAC2 upregulation is associated with hepatocellular carcinoma.
Suggest that HDAC2 can trigger migration and invasion of non-small cell lung carcinoma cells by activating NF-kappaB (show NFKB1 Proteins) to up-regulate fibronectin (show FN1 Proteins) expression.
KLF4 (show KLF4 Proteins) acts as a tumor suppressor or oncogene (show RAB1A Proteins) to activate or repress target gene transcription depending on its acetylation status, which is regulated by p21 (show CDKN1A Proteins) and CK2 (show CSNK2A1 Proteins) interaction-mediated HDAC2 phosphorylation
Data indicate that bombesin receptor (show GRPR Proteins)-activated protein (BRAP (show BRAP Proteins)) might increase histone deacetylases 1/2 (HDAC (show HDAC3 Proteins)) activity that leads to NF-kappa B (NF-kappaB (show NFKB1 Proteins)) activation via its putative C-terminal domain.
Decreased HDAC2 expression is associated with cisplatin resistance in ovarian cancer.
In cigarette smoke extract-exposed airway epithelial cells and macrophages, HDAC2 is excessively ubiquitinated and degraded in the proteasome attributed to low expression of USP17.
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.
We also found that glucocorticoid receptor (GR (show NR3C1 Proteins))-mediated histone deacetylase 2 (HDAC) 2 expression and activity are reduced in the Trpv1 (show TRPV1 Proteins)(-/-) mice and that HDAC2-regulated, cell-cycle- and neuroplasticity-related molecules are altered
CRISPR/Cas9-mediated disruption of the Hdac2 gene increased Slc2a1 expression, suggesting that it is one of the responsible histone deacetylases (HDACs). These results confirm that b-OHB is a HDAC inhibitor and show that b-OHB plays an important role in fasting-induced epigenetic activation of a glucose transporter gene in the brain.
Data suggest that pathological cardiac hypertrophy involved class I histone deacetylases HDAC1 (show HDAC1 Proteins) and HdAC2, tuberous sclerosis complex 2 (TSC2), and mTOR (show FRAP1 Proteins) srine-threonine kinases (mTOR (show FRAP1 Proteins)).
Social isolation resulted in down-regulation of Hdac2 mRNA expression in the cerebral cortex.
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.
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