2. Signaling Pathways
  3. Cell Cycle/DNA Damage
    Epigenetics
  4. HDAC

HDAC

Histone deacetylases

HDAC

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HDAC (Histone deacetylases) are a class of enzymes that remove acetyl groups (O=C-CH3) from an ε-N-acetyl lysine amino acid on ahistone, allowing the histones to wrap the DNA more tightly. This is important because DNA is wrapped around histones, and DNA expression is regulated by acetylation and de-acetylation. Its action is opposite to that of histone acetyltransferase. HDAC proteins are now also called lysine deacetylases (KDAC), to describe their function rather than their target, which also includes non-histone proteins. Together with the acetylpolyamine amidohydrolases and the acetoin utilization proteins, the histone deacetylases form an ancient protein superfamily known as the histone deacetylase superfamily.

HDAC Isoform Specific Products:

HDAC Isoform Comparison
Cat. No. Product Name Effect Purity Chemical Structure
  • HY-130493
    HPB
    		Inhibitor 99.11%
    HPB (HDAC6 inhibitor HPB) is a selective HDAC6 inhibitor with an IC50 of 31 nM. HPB exhibits >30-flod selectivity for HDAC6 over HDAC1.
    HPB
  • HY-162616
    SelSA
    		Inhibitor 99.83%
    SelSA is a selective, orally active inhibitor for histone deacetylase 6 (HDAC6) with IC50 of 56.9 nM. SelSA inhibits the phosphorylation of ERK1/2. SelSA inhibits the proliferation of breast cancer cells and hepatocellular carcinoma cells with IC50 of 0.58-2.6 μM, inhibits cell migration and invasion of Huh7, and induces apoptosis. SelSA exhibits antitumor activity in mouse model.
    SelSA
  • HY-126856
    HC-Toxin
    		Inhibitor 99.26%
    HC-Toxin, a cyclic tetrapeptide, is a potent HDAC inhibitor with an IC50 of 30 nM. HC-Toxin induces tumor cell apoptosis and has anticancer effects.
    HC-Toxin
  • HY-RS06070
    HDAC3 Human Pre-designed siRNA Set A
    		Inhibitor

    HDAC3 Human Pre-designed siRNA Set A contains three designed siRNAs for HDAC3 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
    HDAC3 Human Pre-designed siRNA Set A
  • HY-157388
    CARM1/HDAC2-IN-1
    		Inhibitor
    CARM1/HDAC2-IN-1 (compound CH-1) is a dual inhibitor against CARM1 and HDAC2, with IC50 values of 3.71 nM and 4.07 nM, respectively. CARM1/HDAC2-IN-1 possesses antitumor activity.
    CARM1/HDAC2-IN-1
  • HY-146153
    HDAC-IN-40
    		Inhibitor 98.71%
    HDAC-IN-40 is a potent alkoxyamide-based HDAC inhibitor with Ki values of 60 nM and 30 nM for HDAC2 and HDAC6, respectively. HDAC-IN-40 had antitumor effects.
    HDAC-IN-40
  • HY-117583
    cis-BG47
    		Inhibitor 98.02%
    cis-BG47 is an cis-isomer of BG47, BG47 is a prototypical histone deacetylases HDAC1 and HDAC2 selective, optoepigenetic probe. BG47 can bind to and competitively inhibits the deacetylase activity of HDAC targets upon a light-induced trans-to-cis isomerization, and increases Histone Methyltransferase H3K9 acetylation. cis-BG47 can be used for neurological disease research.
    cis-BG47
  • HY-149669
    PH14
    		Inhibitor 99.29%
    PH14 is a dual PI3K/HDAC inhibitor with IC50 values of 20.3 nM and 24.5 nM for PI3Kα and HDAC3, respectively. PH14 has antiproliferative activity and also induces apoptosis in Jeko-1 cells. PH14 can be used in cancer research, such as lymphoma.
    PH14
  • HY-RS06058
    HDAC1 Human Pre-designed siRNA Set A
    		Inhibitor

    HDAC1 Human Pre-designed siRNA Set A contains three designed siRNAs for HDAC1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
    HDAC1 Human Pre-designed siRNA Set A
  • HY-RS06064
    HDAC11 Human Pre-designed siRNA Set A
    		Inhibitor

    HDAC11 Human Pre-designed siRNA Set A contains three designed siRNAs for HDAC11 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
    HDAC11 Human Pre-designed siRNA Set A
  • HY-149819
    CDK/HDAC-IN-3
    		Inhibitor 99.60%
    CDK/HDAC-IN-3 is an orally active HDACs/CDKs dual inhibitor. CDK/HDAC-IN-3 has potent and selective inhibition of CDK9, CDK12, CDK13, HDAC1, HDAC2 and HDAC3 with IC50 values of 98.32 nM, 98.85 nM, 100 nM, 62.12 nM, 93.28nM and 82.87 nM. CDK/HDAC-IN-3 can be used for the acute myeloid leukemia (AML) .
    CDK/HDAC-IN-3
  • HY-156273
    HDAC/JAK/BRD4-IN-1
    		Inhibitor
    HDAC/JAK/BRD4-IN-1(compound 25ap) is a potent HDAC/JAK/BRD4 triple inhibitor. HDAC/JAK/BRD4-IN-1 inhibit cell growth and induces apoptosis in MDA-MB-231 cells, and shows anticancer activity in vivo.
    HDAC/JAK/BRD4-IN-1
  • HY-RS06067
    HDAC2 Human Pre-designed siRNA Set A
    		Inhibitor

    HDAC2 Human Pre-designed siRNA Set A contains three designed siRNAs for HDAC2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
    HDAC2 Human Pre-designed siRNA Set A
  • HY-159045
    F-SAHA
    		Inhibitor 99.90%
    F-SAHA is a HDAC inhibitor (HDACi) and its 18F labeled derivative can be used in tumor imaging research.
    F-SAHA
  • HY-156096
    HDAC3-IN-2
    		Inhibitor
    HDAC3-IN-2 (compound 4i) is a pyrazinyl hydrazide-based HDAC3 inhibitor (IC50: 14 nM) that efficiently targets triple-negative breast cancer cells. HDAC3-IN-2 is cytotoxic with an IC50 of 0.55 μM against 4T1 and an IC50 of 0.74 μM against MDA-MB-231. HDAC3-IN-2 has anti-tumor efficacy in vivo in tumor-bearing mouse models, selectively increasing the acetylation levels of H3K9, H3K27 and H4K12, increasing the contents of apoptosis-related caspase-3, caspase-7 and cytochrome c, and reducing Proliferation-related Bcl-2, CD44, EGFR, and Ki-67 levels.
    HDAC3-IN-2
  • HY-161304
    HDAC6-IN-33
    		Inhibitor 98.96%
    HDAC6-IN-33 (compound 6) is a selective and irreversible HDAC6 inhibitor with an IC50 of 193 nM. HDAC6-IN-33 shows no activity against HDAC1-4. HDAC6-IN-33 is a tight-binding HDAC6 inhibitor capable of inhibiting HDAC6 via a two-step slow-binding mechanism.
    HDAC6-IN-33
  • HY-128763
    HDAC-IN-4
    		Inhibitor 98.00%
    HDAC-IN-4 is a selective HDAC6 and HDAC10 inhibitor with pIC50s of 7.2 and 6.8 in BRET assay, respectively. Antitumoral activity.
    HDAC-IN-4
  • HY-124782
    HDAC8-IN-8
    		Inhibitor 99.01%
    HDAC8-IN-8 (15a) is an HDAC8 inhibitor, with IC50 values of 23.9 μM and 268.2 μM for hHDAC8 and smHDAC8 respectively. And for hHDAC1 and hHDAC6, the IC50 values are 12.1 μM and 2.9 μM respectively. HDAC8-IN-8 can be used in schistosomiasis-related research.
    HDAC8-IN-8
  • HY-156602
    Bocodepsin
    		Inhibitor 98.01%
    Bocodepsin (OKI-179) is an orally active and selective HDAC inhibitor, with antitumor activity. Bocodepsin can be used for suppression on solid tumor and hematologic malignancies.
    Bocodepsin
  • HY-173053
    HDAC-IN-87
    		Inhibitor 99.89%
    HDAC-IN-87 (Compound XII6) is a nonselective HDAC inhibitor, with pIC50 of 6.9 (HDAC4) and 5.8 (HDAC6) respectively. HDAC-IN-87 has fungicidal activity against P. sorghi and P. pachyrhizi. HDAC-IN-87 shows an acute oral LD50 of greater than 500 mg/kg in male and female rats.
    HDAC-IN-87
Cat. No. Product Name / Synonyms Application Reactivity
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Download HDAC Signaling Pathway Map.

TCR, GPCR and HDAC II interaction: Diverse agonists act through G-protein-coupled receptors (GPCRs) to activate the PKC-PKD axis, CaMK, Rho, or MHC binding to antigens stimulates TCR to activate PKD, leading to phosphorylation of class II HDACs. Phospho-HDACs dissociate from MEF2, bind 14-3-3, and are exported to the cytoplasm through a CRM1-dependent mechanism. CRM1 is inhibited by leptomycin B (LMB). Release of MEF2 from class II HDACs allows p300 to dock on MEF2 and stimulate gene expression. Dephosphorylation of class II HDACs in the cytoplasm enables reentry into the nucleus[1].

 

TLR: TLR signaling is initiated by ligand binding to receptors. The recruitment of TLR domain-containing adaptor protein MyD88 is repressed by HDAC6, whereas NF-κB and MTA-1 can be negatively regulated by HDAC1/2/3 and HDAC2, respectively. Acetylation by HATs enhance MKP-1 which inhibits p38-mediated inflammatory responses, while HDAC1/2/3 inhibits MKP-1 activity. HDAC1 and HDAC8 repress, whereas HDAC6 promotes, IRF function in response to viral challenge. HDAC11 inhibits IL-10 expression and HDAC1 and HDAC2 represses IFNγ-dependent activation of the CIITA transcription factor, thus affecting antigen presentation[2][3].

 

IRNAR: IFN-α/β induce activation of the type I IFN receptor and then bring the receptor-associated JAKs into proximity. JAK adds phosphates to the receptor. STATs bind to the phosphates and then phosphorylated by JAKs to form a dimer, leading to nuclear translocation and gene expression. HDACs positively regulate STATs and PZLF to promote antiviral responses and IFN-induced gene expression[2][3].

 

Cell cycle: In G1 phase, HDAC, Retinoblastoma protein (RB), E2F and polypeptide (DP) form a repressor complex. HDAC acts on surrounding chromatin, causing it to adopt a closed chromatin conformation, and transcription is repressed. Prior to the G1-S transition, phosphorylation of RB by CDKs dissociates the repressor complex. Transcription factors (TFs) gain access to their binding sites and, together with the now unmasked E2F activation domain. E2F is then free to activate transcription by contacting basal factors or by contacting histone acetyltransferases, such as CBP, that can alter chromatin structure[4].

 

The function of non-histone proteins is also regulated by HATs/HDACs. p53: HDAC1 impairs the function of p53. p53 is acetylated under conditions of stress or HDAC inhibition by its cofactor CREB binding protein (CBP) and the transcription of genes involved in differentiation is activated. HSP90: HSP90 is a chaperone that complexes with other chaperones, such as p23, to maintain correct conformational folding of its client proteins. HDAC6 deacetylates HSP90. Inhibition of HDAC6 would result in hyperacetylated HSP90, which would be unable to interact with its co-chaperones and properly lead to misfolded client proteins being targeted for degradation via the ubiquitin-proteasome system[5][6].
 

Reference:

[1]. Vega RB, et al. Protein kinases C and D mediate agonist-dependent cardiac hypertrophy through nuclear export of histone deacetylase 5.Mol Cell Biol. 2004 Oct;24(19):8374-85.
[2]. Shakespear MR, et al. Histone deacetylases as regulators of inflammation and immunity. Trends Immunol. 2011 Jul;32(7):335-43.
[3]. Suliman BA, et al. HDACi: molecular mechanisms and therapeutic implications in the innate immune system.Immunol Cell Biol. 2012 Jan;90(1):23-32. 
[4]. Brehm A, et al. Retinoblastoma protein meets chromatin.Trends Biochem Sci. 1999 Apr;24(4):142-5.
[5]. Butler R, et al. Histone deacetylase inhibitors as therapeutics for polyglutamine disorders.Nat Rev Neurosci. 2006 Oct;7(10):784-96
[6]. Minucci S, et al. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer.Nat Rev Cancer. 2006 Jan;6(1):38-51.

HDAC Isoform Comparison

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