You Searched For: Histone+Deacetylase+Inhibitor+VIII

Catalog Number: (BOSSBS-11275R-A750)

Supplier: Bioss

Description: CtBP1 associates in complexes with histone deacetylases (HDAC), the G9a histone methyltransferase, and LSD1 histone demethylase illustrating its role in transcriptional repression. Through its association with centrosomes, CtBP1 appears to also play a role in mitosis and Golgi complex organization.

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Catalog Number: (BOSSBS-3073R-A680)

Supplier: Bioss

Description: 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 class II histone deacetylase/acuc/apha family. It possesses histone deacetylase activity and represses transcription when tethered to a promoter. It coimmunoprecipitates only with HDAC3 family member and might form multicomplex proteins. It also interacts with myocyte enhancer factor-2 (MEF2) proteins, resulting in repression of MEF2-dependent genes. This gene is thought to be associated with colon cancer. Two transcript variants encoding different isoforms have been found for this gene.

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Catalog Number: (BOSSBS-2893R-CY5.5)

Supplier: Bioss

Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.

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Catalog Number: (BOSSBS-11275R-A555)

Supplier: Bioss

Description: CtBP1 associates in complexes with histone deacetylases (HDAC), the G9a histone methyltransferase, and LSD1 histone demethylase illustrating its role in transcriptional repression. Through its association with centrosomes, CtBP1 appears to also play a role in mitosis and Golgi complex organization.

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Catalog Number: (BOSSBS-2893R-CY7)

Supplier: Bioss

Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.

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Catalog Number: (BOSSBS-2809R-A647)

Supplier: Bioss

Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer.

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Catalog Number: (BOSSBS-7134R-HRP)

Supplier: Bioss

Description: This gene encodes a protein that may modulate the transcriptional repression activities of death-associated protein 6 (DAXX), which interacts with histone deacetylase, core histones, and other histone-associated proteins. In mouse, the encoded protein binds to the putative leucine zipper domain of macroH2A1.2, a variant H2A histone that is enriched on inactivated X chromosomes. The BTB/POZ domain of this protein has been shown in other proteins to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes. Alternative splicing of this gene results in multiple transcript variants encoding the same protein. [provided by RefSeq, Jul 2008].

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Catalog Number: (BOSSBS-3216R)

Supplier: Bioss

Description: HDAC7 is a member of the class II mammalian histone deacetylases, which plays an important role in modulating the eukaryotic chromatin structure. Human HDAC7 is composed of 912 amino acid residues. Although HDAC7 is localized mostly to the cell nucleus, it is also found in the cytoplasm, suggesting nucleo-cytoplasmic shuttling. The histone deacetylase activity of HDAC7 maps to a carboxy-terminal domain and is dependent on interaction with class I HDACs in the nucleus. It is an active component of different transcriptional corepressor complexes that can be recruited to specific promoter regions via interactions with a growing number of sequence specific transcriptional factors. HDAC7 catalyzes removal of acetyl-groups from acetyl-lysines of histones and promotes compaction of chromatin in these regions, leading to the inhibition of gene transcription.

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Catalog Number: (BOSSBS-3216R-A647)

Supplier: Bioss

Description: HDAC7 is a member of the class II mammalian histone deacetylases, which plays an important role in modulating the eukaryotic chromatin structure. Human HDAC7 is composed of 912 amino acid residues. Although HDAC7 is localized mostly to the cell nucleus, it is also found in the cytoplasm, suggesting nucleo-cytoplasmic shuttling. The histone deacetylase activity of HDAC7 maps to a carboxy-terminal domain and is dependent on interaction with class I HDACs in the nucleus. It is an active component of different transcriptional corepressor complexes that can be recruited to specific promoter regions via interactions with a growing number of sequence specific transcriptional factors. HDAC7 catalyzes removal of acetyl-groups from acetyl-lysines of histones and promotes compaction of chromatin in these regions, leading to the inhibition of gene transcription.

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Catalog Number: (BOSSBS-5634R-CY7)

Supplier: Bioss

Description: NAD-dependent protein deacetylase. Has deacetylase activity towards histone H3K9Ac and H3K56Ac. Modulates acetylation of histone H3 in telomeric chromatin during the S-phase of the cell cycle. Deacetylates histone H3K9Ac at NF-kappa-B target promoters and may down-regulate the expression of a subset of NF-kappa-B target genes. Acts as a corepressor of the transcription factor HIF1A to control the expression of multiple glycolytic genes to regulate glucose homeostasis. Required for genomic stability. Regulates the production of TNF protein. Has a role in the regulation of life span (By similarity). Deacetylation of nucleosomes interferes with RELA binding to target DNA. May be required for the association of WRN with telomeres during S-phase and for normal telomere maintenance. Required for genomic stability. Required for normal IGF1 serum levels and normal glucose homeostasis. Modulates cellular senescence and apoptosis. On DNA damage, promotes DNA end resection via deacetylation of RBBP8. Has very weak deacetylase activity and can bind NAD(+) in the absence of acetylated substrate.

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Catalog Number: (BOSSBS-7962R)

Supplier: Bioss

Description: Ankyrin repeats containing cofactors may recruit histone deacetylases to the p160 coactivators/nuclear receptor complex to inhibit ligand-dependent transactivation.

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Catalog Number: (BOSSBS-1813R-A555)

Supplier: Bioss

Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation. Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A.

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Catalog Number: (BOSSBS-5634R-A350)

Supplier: Bioss

Description: NAD-dependent protein deacetylase. Has deacetylase activity towards histone H3K9Ac and H3K56Ac. Modulates acetylation of histone H3 in telomeric chromatin during the S-phase of the cell cycle. Deacetylates histone H3K9Ac at NF-kappa-B target promoters and may down-regulate the expression of a subset of NF-kappa-B target genes. Acts as a corepressor of the transcription factor HIF1A to control the expression of multiple glycolytic genes to regulate glucose homeostasis. Required for genomic stability. Regulates the production of TNF protein. Has a role in the regulation of life span (By similarity). Deacetylation of nucleosomes interferes with RELA binding to target DNA. May be required for the association of WRN with telomeres during S-phase and for normal telomere maintenance. Required for genomic stability. Required for normal IGF1 serum levels and normal glucose homeostasis. Modulates cellular senescence and apoptosis. On DNA damage, promotes DNA end resection via deacetylation of RBBP8. Has very weak deacetylase activity and can bind NAD(+) in the absence of acetylated substrate.

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Catalog Number: (BOSSBS-3216R-A750)

Supplier: Bioss

Description: HDAC7 is a member of the class II mammalian histone deacetylases, which plays an important role in modulating the eukaryotic chromatin structure. Human HDAC7 is composed of 912 amino acid residues. Although HDAC7 is localised mostly to the cell nucleus, it is also found in the cytoplasm, suggesting nucleo-cytoplasmic shuttling. The histone deacetylase activity of HDAC7 maps to a carboxy-terminal domain and is dependent on interaction with class I HDACs in the nucleus. It is an active component of different transcriptional corepressor complexes that can be recruited to specific promoter regions via interactions with a growing number of sequence specific transcriptional factors. HDAC7 catalyses removal of acetyl-groups from acetyl-lysines of histones and promotes compaction of chromatin in these regions, leading to the inhibition of gene transcription.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-2811R-A680)

Supplier: Bioss

Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that Recognises polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-2811R-A750)

Supplier: Bioss

Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that Recognises polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.

UOM: 1 * 100 µl

Sale