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These data provide support for the hypothesis that HDAC8 may undergo metal switching in vivo that, in turn, may regulate its activity. However, future studies are needed to explore the identity of the metal ion bound to HDAC8 in cells under varied conditions
The study reports the crystal structure of the HDAC8-trapoxin A complex at 1.24 A resolution, revealing that the ketone moiety of l-Aoe undergoes nucleophilic attack to form a zinc-bound tetrahedral gem (show GEM ELISA Kits)-diolate that mimics the tetrahedral intermediate and its flanking transition states in catalysis.
The findings suggest that miR (show MLXIP ELISA Kits)-455-3p plays a critical role during chondrogenesis by directly targeting HDAC2 (show HDAC2 ELISA Kits)/8 and promoting histone H3 (show HIST3H3 ELISA Kits) acetylation.
7-amino-4-methylcoumarin did not affect acetyllysine preference in a multiply acetylated substrate. In contrast, AMC significantly enhanced KDAC6 substrate affinity, greatly reduced Sirt1 (show SIRT1 ELISA Kits) activity, eliminated the substrate sequence specificity of KDAC4, and had no consistent effect with KDAC8 substrates.
Enzymological, biophysical, and structural studies of Cornelia de Lange Syndrome HDAC8 protein mutants have yielded critical insight on compromised catalysis in vitro. Most CdLS (show NIPBL ELISA Kits) HDAC8 mutations trigger structural changes that directly or indirectly impact substrate binding and catalysis.
class I HDACs (HDAC1 (show HDAC1 ELISA Kits), 2, 3 and 8) play a major role in regulating extracellular matrix and Epithelial-mesenchymal transition, whereas class IIa HDACs (HDAC4 (show HDAC4 ELISA Kits) and 5) are less effective.
Losses of catalytic efficiency in histone deacetylase 8 (HDAC8) are observed for G304A and G305A mutations.
Data suggest sequencing of histone deacetylase 8 protein (HDAC8) as an indispensable part of the routine molecular diagnostic for patients with Cornelia de Lange syndrome (CdLS (show NIPBL ELISA Kits)) or CdLS (show NIPBL ELISA Kits)-overlapping features.
HDAC8 were overexpressed in oral squamous cell carcinoma tissues, mainly localized in the cytoplasm.
Study reveals that HDAC8 can bind and catalyze deacetylation of many acetylated peptides with sequences corresponding to cellular, non-histone proteins, thereby opening a new window to the functional role of HDAC8 in cells.
this study demonstrates a novel role of HDAC8 in LeTx immunotoxicity and regulation of pro-IL-1beta (show IL1B ELISA Kits) production likely through eRNAs.
findings show how HDAC8 drives nonalcoholic fatty liver disease-associated hepatocarcinogenesis
Data reveal a role for miR (show MLXIP ELISA Kits)-21-3p in regulating HDAC8 expression and Akt (show AKT1 ELISA Kits)/Gsk3beta (show GSK3b ELISA Kits) pathway in cardiac hypertrophy.
histone deacetylase 8 inhibition reduces gene expression and production of proinflammatory cytokines in vitro and in vivo
HDAC8 and Sirt1 (show SIRT1 ELISA Kits) were also demonstrated to interact directly with ERRalpha (show ESRRA ELISA Kits) in vivo and to deacetylate and increase the DNA binding affinity of ERRalpha (show ESRRA ELISA Kits) in vitro.
Global deletion of Hdac8 in mice leads to perinatal lethality due to skull instability, and deletion of Hdac8 in cranial neural crest cells and Hdac8 specifically represses the aberrant expression of homeobox (show PRRX1 ELISA Kits) transcription factors such as Otx2 (show OTX2 ELISA Kits) and Lhx1 (show LHX1 ELISA Kits)
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 class I of the histone deacetylase family. It catalyzes the deacetylation of lysine residues in the histone N-terminal tails and represses transcription in large multiprotein complexes with transcriptional co-repressors. Multiple transcript variants encoding different isoforms have been found for this gene.
histone deacetylase 8
, histone deacetylase-like 1