You Searched For: Nepsilon-acetyl-L-lysine

Catalog Number: (10087-614)

Supplier: Proteintech

Description: Histone deacetylases(HDAC) are a class of enzymes that remove the acetyl groups from the lysine residues leading to the formation of a condensed and transcriptionally silenced chromatin. At least 4 classes of HDAC were identified. HDAC6 is a member of the class II mammalian histone deacetylases. It possesses two separate putative catalytic domains. Both catalytic domains are fully functional HDACs and contribute independently to the overall activity of HDAC6 protein. A very potent NES is present at the amino-terminus of HDAC6, which was found to play an important role in regulating the shuttling of HDAC6 protein between cytoplasm and nucleus. The shuttling process may be a critical regulatory mechanism of HDAC6 function. The expression of HDAC6 is tightly linked to the state of cell differentiation. HDAC6 may participate in coordinating expression of a group of genes involved in the remodelling of chromatin during cell differentiation. This antibody is specific to HDAC6. It does not cross react with other HDACs.

Catalog Number: (10068-440)

Supplier: Prosci

Description: Histone Deacetylases (HDACs) are a group of enzymes closely related to sirtuins. They catalyze the removal of acetyl groups from lysine residues in histones and non-histone proteins, resulting in transcriptional repression. In general, they do not act autonomously but as components of large multiprotein complexes, such as pRb-E2F and mSin3A, that mediate important transcription regulatory pathways. There are three classes of HDACs; classes 1, 2 and 4, which are closely related Zn2+-dependent enzymes. HDACs are ubiquitously expressed and they can exist in the nucleus or cytosol. Their subcellular localization is effected by protein-protein interactions (for example HDAC-14.3.3 complexes are retained in the cytosol) and by the class to which they belong (class 1 HDACs are predominantly nuclear whilst class 2 HDACs shuttle between the nucleus and cytosol). HDACs have a role in cell growth arrest, differentiation and death and this has led to substantial interest in HDAC inhibitors as possible antineoplastic agents.

Catalog Number: (89359-244)

Supplier: Genetex

Description: CBP and p300 are large nuclear proteins that bind to many sequence-specific factors involved in cell growth and/or differentiation, including c-jun and the adenoviral oncoprotein E1A. The protein encoded by this gene associates with p300/CBP. It has in vitro and in vivo binding activity with CBP and p300, and competes with E1A for binding sites in p300/CBP. It has histone acetyl transferase activity with core histones and nucleosome core particles, indicating that this protein plays a direct role in transcriptional regulation.

Catalog Number: (10078-780)

Supplier: Prosci

Description: Histone deacetylase (HDAC) and histone acetyltransferase (HAT) are enzymes that regulate transcription by selectively deacetylating or acetylating the eta-amino groups of lysines located near the amino termini of core histone proteins. Eight members of HDAC family have been identified in the past several years. These HDAC family members are divided into two classes, I and II. Class I of the HDAC family comprises four members, HDAC-1, 2, 3, and 8, each of which contains a deacetylase domain exhibiting from 45 to 93% identity in amino acid sequence. Class II of the HDAC family comprises HDAC-4, 5, 6, and 7, the molecular weights of which are all about twofold larger than those of the class I members, and the deacetylase domains are present within the C-terminal regions, except that HDAC-6 contains two copies of the domain, one within each of the N-terminal and C-terminal regions. Human HDAC-1, 2 and 3 were expressed in various tissues, but the others (HDAC-4, 5, 6, and 7) showed tissue-specific expression patterns. These results suggested that each member of the HDAC family exhibits a different, individual substrate specificity and function in vivo.

Catalog Number: (77437-594)

Supplier: Bioss

Description: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Regulation of gene expression levels depends on the balance between methylation and acetylation levels of tha CTD-lysines (By similarity). Initiation or early elongation steps of transcription of growth-factors-induced immediate early genes are regulated by the acetylation status of the CTD (PubMed:24207025). Methylation and dimethylation have a repressive effect on target genes expression

Catalog Number: (75794-160)

Supplier: Prosci

Description: TIP60 is the catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex is required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. TIP60 directly acetylates and activates ataxia-telangiectasia mutated (ATM). In case of HIV-1 infection, interaction with the viral Tat protein leads to KAT5 polyubiquitination and targets it to degradation.

Catalog Number: (89359-226)

Supplier: Genetex

Description: The basic repeating unit of chromatin is the nucleosome, which is composed of a protein octamer containing two each of the core histones H2A, H2B, H3, and H4, surrounded by approximately 146 base pairs of DNA. Reversible acetylation of highly conserved lysine residues in the N-terminal tail domains of core histones plays an important role in transcriptional regulation, cell cycle progression, and development events. Several histone acetyltransferases (HATs) catalyze this acetylation reaction (e.g. GCN5, PCAF, p300/CBP, TAFII250, P/CAF, SRC-1, BRCA-2). Acetylation of the core histones is generally considered to be associated with gene activation, probably through maintenance of the unfolded structure of transcribing nucleosomes. Histone acetylation is a dynamic process in which levels are determined by the net activities of HATs and the competing enzymes histone deacetylases (HDACs). Both activities are associated with the nuclear matrix. Eleven different mammalian HDACs have been described. HDACs 1-3 & 8 (Class I) are similar to yeast Rpd3 protein, while HDACs 4-7, 9 & 10 (Class II) are similar to yeast Hda1 protein. The activities of the histone deacetylases are often, but not always, associated with transcriptional repression and nucleosome condensation. HDAC1, HDAC2 and several others are the catalytic subunits of different multiprotein regulatory complexes. Other components of such complexes may include: corepressors such as mSin3, N-CoR, SMRT, associated proteins such as SAP18, SAP30, RbAp46, RbAp48, and c-Ski oncogenic protein (involved in DNA methylation). Nucleosome remodeling and deacetylation (NRD) complexes containing HDAC1, HDAC2, Mi-2 (CH3, CH4) dermatomyositis specific autoantigen, and MAT2 (metastasis-associated protein) (related to MAT1) have been described. It is therefore assumed that ATP-dependent nucleosome remodeling activity and histone deacetylation may be interconnected or interdependent. Recruitment of the multiprotein complexes to promoter sites occurs by many sequence specific DNA-binding proteins such as unliganded nuclear hormone receptors, DP1-E2F, YY1, and Rb family of transcription factors, transcriptional repressors, and tumor suppressors (e.g. BRCA1). Aberrant recruitment of HDACs by various oncoproteins may occur in certain neoplastic diseases. It has been found that inhibition ofHDAC2 activity by valporic acid induces proteosomal degradation of HDAC2.

Catalog Number: (10091-284)

Supplier: Proteintech

Description: Steroidogenic factor-1 (SF-1,STF-1), also known as NR5A1, regulates multiple genes involved in the adrenal and gonadal development and in the biosynthesis of a variety of hormones, including adrenal and gonadal steroids, anti-Mullerian hormone (AMH), and gonadotropins. SF-1 belongs to the fushi tarazu factor-1 (FTZ-F1) subfamily of orphan nuclear receptors. Initially identified as a tissue-specific transcriptional regulator of cytochrome P450 steroid hydroxylases, research studies of both global and tissue-specific knockout mice have demonstrated that SF-1 is required for the development of adrenal glands, gonads, ventromedial hypothalamus, and for the proper functioning of pituitary gonadotropes. Indeed, humans with mutations that render SF-1 transcriptionally inactive can present with testicular failure, ovarian failure, and adrenal insufficiency. Furthermore, dysregulation of SF-1 has been linked to diseases such as endometriosis and adrenocortical carcinoma.Like other nuclear hormone receptors, SF-1 has a modular domain structure composed of an N-terminal zinc finger DNA-binding domain, a ligand-binding domain, a C-terminal AF-2 activation domain, and a hinge region with AF-1-like activation activity. SF-1 also contains a fushi tarazu factor 1 box, which functions as an accessory DNA binding domain. SF-1 is primarily phosphorylated at Ser203, which is thought to enhance its transcriptional activity by promoting complex formation with transcriptional cofactors. In addition to phosphorylation at Ser203, SF-1 is subject to SUMO conjugation and acetylation at ε-amino groups of target lysine residues. Whereas SUMOylation represses SF-1 function, acetylation enhances its transcriptional activity.In the adult ovary, SF-1 localizes to theca/interstitial cells.

Catalog Number: (CARL600401I89)

Supplier: Rockland Immunochemical

Description: Anti-Histone H3 [ac Lys36] antibody is useful for Western Blot and Dot Blot. Specific conditions for reactivity should be optimized by the end user. Expect a band approximately ~15.4 kDa corresponding to Histone H3 protein by Western Blotting in HeLa hist

Catalog Number: (10087-612)

Supplier: Proteintech

Description: Histone deacetylases(HDAC) are a class of enzymes that remove the acetyl groups from the lysine residues leading to the formation of a condensed and transcriptionally silenced chromatin. At least 4 classes of HDAC were identified. HDAC6 is a member of the class II mammalian histone deacetylases. It possesses two separate putative catalytic domains. Both catalytic domains are fully functional HDACs and contribute independently to the overall activity of HDAC6 protein. A very potent NES is present at the amino-terminus of HDAC6, which was found to play an important role in regulating the shuttling of HDAC6 protein between cytoplasm and nucleus. The shuttling process may be a critical regulatory mechanism of HDAC6 function. The expression of HDAC6 is tightly linked to the state of cell differentiation. HDAC6 may participate in coordinating expression of a group of genes involved in the remodelling of chromatin during cell differentiation. HDAC6 has some splicing variants such as P114(~130kd), P131(~160kd).This antibody is a rabbit polyclonal antibody raised against residues near the C terminal of human HDAC6.

Catalog Number: (77440-186)

Supplier: Bioss

Description: Histone acetylation and deacetylation, catalyzed by multisubunit complexes, play a key role in the regulation of eukaryotic gene expression. The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family and is a component of the histone deacetylase complex. It also interacts with retinoblastoma tumor-suppressor protein and this complex is a key element in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2, it deacetylates p53 and modulates its effect on cell growth and apoptosis. (provided by RefSeq, Jul 2008)
Function : 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. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Component a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development.

Catalog Number: (89156-514)

Supplier: Enzo Life Sciences

Description: A Fluor de Lys® fluorescent assay system

Catalog Number: (89156-512)

Supplier: Enzo Life Sciences

Description: A Fluor de Lys® fluorescent assay system

Supplier: AVANTOR PERFORMANCE MATERIAL LLC

Description: L(+)-Lysine monohydrochloride 98.5-101.5% (dried basis), GenAR® USP, Multi-Compendial, Macron Fine Chemicals™

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Supplier: Thermo Scientific Chemicals

Description: L(+)-Lysine monohydrate 97%

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Supplier: Thermo Scientific Chemicals

Description: L(+)-Lysine dihydrochloride 99%

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