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Mouse (Murine) HDAC8 Protein expressed in Baculovirus infected Insect Cells - ABIN2007594
Hu, Chen, Fredrickson, Zhu, Kirkpatrick, Zhang, Johanson, Sung, Liu, Winkler: Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor. in The Journal of biological chemistry 2000
Show all 3 references for ABIN2007594
Human HDAC8 Protein expressed in Baculovirus infected Insect Cells - ABIN2003497
Buggy, Sideris, Mak, Lorimer, McIntosh, Clark: Cloning and characterization of a novel human histone deacetylase, HDAC8. in The Biochemical journal 2001
Show all 3 references for ABIN2003497
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 Proteins)) or CdLS (show NIPBL Proteins)-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.
Findings suggest the therapeutic potential of histone deacetylase 8 histone (HDAC8)inhibition to suppress Notch1 (show NOTCH1 Proteins) signaling in breast cancer.
Data show that histone deacetylase 8 (HDAC8) inhibition led to accumulation of acetylated-SMC3 (show SMC3 Proteins) protein but had no influence on the transcription of estrogen-responsive genes.
study elucidates an HDAC8-mediated p53 (show TP53 Proteins)-inactivating mechanism promoting leukemia stem cells activity
Studies indicate that histone deacetylase 8 protein (HDAC8) aberrantly deacetylates p53 (show TP53 Proteins) protein and promotes leukemia stem cells (LSCs) transformation and maintenance.
Our data exhibited an important role of HDAC8 in promoting gastric cancer tumorigenesis and identify this HDAC8 as a potential therapeutic target for the treatment of gastric cancer.
The H143A and H142A/H143A mutants exhibit activity that is >80000-fold lower than that of wild-type HDAC8; the buried D176N and D176A mutants have significant catalytic effects, with more subtle effects caused by D183N and D183A
this study demonstrates a novel role of HDAC8 in LeTx immunotoxicity and regulation of pro-IL-1beta (show IL1B Proteins) production likely through eRNAs.
findings show how HDAC8 drives nonalcoholic fatty liver disease-associated hepatocarcinogenesis
Data reveal a role for miR-21-3p in regulating HDAC8 expression and Akt/Gsk3beta 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 Proteins) were also demonstrated to interact directly with ERRalpha (show ESRRA Proteins) in vivo and to deacetylate and increase the DNA binding affinity of ERRalpha (show ESRRA Proteins) 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 Proteins) transcription factors such as Otx2 (show OTX2 Proteins) and Lhx1 (show LHX1 Proteins)
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