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

HDAC

Histone deacetylases

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.

Cat. No. Product Name Effect Purity Chemical Structure
  • HY-156027
    SIRT6-IN-3
    Inhibitor 98.19%
    SIRT6-IN-3 (compound 8a) is a selective inhibitor of SIRT6 (IC50=7.49 μM). SIRT6-IN-3 inhibits pancreatic ductal adenocarcinoma (PDAC) cells proliferation and induces apoptosis. SIRT6-IN-3 increases the sensitivity of cancer cells to gemcitabine (HY-17026) via blocking the DNA damage repair pathway. SIRT6-IN-3 is used in pancreatic cancer research.
    SIRT6-IN-3
  • HY-141427
    MOCPAC
    99.64%
    MOCPAC is an HDAC1 specific substrate.
    MOCPAC
  • HY-149208
    HDAC-IN-53
    Inhibitor
    HDAC-IN-53 is an orally active, and selective HDAC1-3 inhibitor with IC50 values of 47 nM, 125 nM, and 450 nM, respectively. HDAC-IN-53 does not inhibit class II HDACs (HDAC4, 5, 6, 7, 9; IC50>10 μM). HDAC-IN-53 induces caspase-dependent apoptosis. HDAC-IN-53 significantly inhibits the growth of human tumor xenografts in nude mice and murine tumor growth in immune-competent mice bearing MC38 colon cancer.
    HDAC-IN-53
  • HY-13592
    HDAC-IN-7
    Inhibitor
    HDAC-IN-7 (Chidamide impurity) is an impurity of Chidamide. Chidamide is a potent and orally bioavailable HDAC enzymes class I (HDAC1/2/3) and class IIb (HDAC10) inhibitor.
    HDAC-IN-7
  • HY-152174
    HDAC-IN-52
    Inhibitor 99.46%
    HDAC-IN-52 is a pyridine-containing HDAC inhibitor, with IC50s of 0.189, 0.227, 0.440 and 0.446 μM for HDAC1, HDAC2, HDAC3, and HDAC10, respectively. HDAC-IN-52 can be used for the research of cancer.
    HDAC-IN-52
  • 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-120448
    QTX125
    Inhibitor
    QTX125 is a potent and highly selective HDAC6 inhibitor. QTX125 exhibits excellent selectivity over other HDACs. QTX125 has antitumor effects.
    QTX125
  • HY-120448A
    QTX125 TFA
    Inhibitor 99.93%
    QTX125 TFA is a potent and highly selective HDAC6 inhibitor. QTX125 TFA exhibits excellent selectivity over other HDACs. QTX125 has antitumor effects.
    QTX125 TFA
  • HY-156258
    HDAC6-IN-21
    Inhibitor 99.44%
    HDAC6-IN-21 (compound 13) is airreversibleinhibitor of histonedeacetylase 6 (HDAC6).
    HDAC6-IN-21
  • 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-162361
    HDAC1-IN-7
    Inhibitor
    HDAC1-IN-7 (compound 9) is potent HDAC1 inhibitor, with the IC50 of 0.957 mM.
    HDAC1-IN-7
  • HY-174444
    PROTAC HDAC degrader-2
    Degrader
    PROTAC HDAC degrader-2 is a selective IIb HDACs PROTAC degrader, with DC50s of 13 nM for HDAC6, 29 nM for HDAC10, respectively. PROTAC HDAC degrader-2 exhibits low cytotoxicity against hematological and solid cancer cell lines. PROTAC HDAC degrader-2 can be used for the chemical knockdown of class IIb HDACs. ( Pink: HDAC ligand : (HY-174471), Blue: E3 ligase CRBN Ligand (HY-131717), E3 ligase ligand-linker conjugate (HY-174473)).
    PROTAC HDAC degrader-2
  • HY-P3242
    Mad1 (6-21)
    98.02%
    Mad1 (6-21) is the 6-21 fragment of Mad1 protein. Mad1 (6-21) binds to mammalian Sin3A PAH2 with a Kd of ~29 nM.
    Mad1 (6-21)
  • HY-131961
    Triciferol
    Antagonist 98.61%
    Triciferol functions as a multiple ligand with combined VDR agonist and HDAC antagonist activities. Triciferol binds directly to the VDR (IC50=87 nM), and functions as an agonist with 1,25D-like potency on several 1,25D target genes. Triciferol induces marked tubulin hyperacetylation, and augments histone acetylation. Antiproliferative and cytotoxic activities.
    Triciferol
  • HY-126141
    JAK/HDAC-IN-1
    Inhibitor 98.63%
    JAK/HDAC-IN-1 is a potent JAK2/HDAC dual inhibitor, exhibits antiproliferative and proapoptotic activities in several hematological cell lines. JAK/HDAC-IN-1 shows IC50s of 4 and 2 nM for JAK2 and HDAC, respectively.
    JAK/HDAC-IN-1
  • HY-RS06085
    HDAC8 Human Pre-designed siRNA Set A
    Inhibitor

    HDAC8 Human Pre-designed siRNA Set A contains three designed siRNAs for HDAC8 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.

    HDAC8 Human Pre-designed siRNA Set A
  • HY-159109
    HDAC6-IN-46
    Inhibitor 98.51%
    HDAC6-IN-46 (compound 12) is a selective histone deacetylase 6 (HDAC6) inhibitor with an IC50 value of 6.2 nM. HDAC6-IN-46 can be used in Alzheimer's disease research.
    HDAC6-IN-46
  • HY-15654S
    Phenylbutyrate-d11 sodium
    Inhibitor 99.85%
    Phenylbutyrate-d11 (sodium) is deuterium labeled Sodium 4-phenylbutyrate. Sodium 4-phenylbutyrate (4-PBA sodium) is an inhibitor of HDAC and endoplasmic reticulum (ER) stress, used in cancer and infection research.
    Phenylbutyrate-d<sub>11</sub> sodium
  • HY-151261
    HDAC6-IN-13
    Inhibitor 98.08%
    HDAC6-IN-13 (Compound 35m) is a potent, highly selective, orally active HDAC6 inhibitor with an IC50 of 0.019 μM. HDAC6-IN-13 also inhibits HDAC1, HDAC2 and HDAC3 with IC50s of 1.53, 2.06 and 1.03 μM, respectively. HDAC6-IN-13 shows significant BBB permeability and anti-inflammatory activity.
    HDAC6-IN-13
  • HY-128919
    Ac-Lys-AMC
    98.93%
    Ac-Lys-AMC (Hexanamide), also termed MAL, is a fluorescent substrate for histone deacetylase HDACs.
    Ac-Lys-AMC
Cat. No. Product Name / Synonyms Application Reactivity

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.

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