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AB120850

Trichostatin A, histone deacetylase inhibitor

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(5 Publications)

MW 302.37 Da, Purity >98%. Potent, selective histone deacetylase (HDAC) inhibitor (Ki = 3.4 nM). Induces cell proliferation, differentiation and apoptosis in vitro. Anticancer and antifungal agent. Active in vivo and in vitro.

View Alternative Names

2810449N18Rik, ABC 35, ABCC 7, AHDC, AHO3, AI043036, ALDC, ALDH 1, ALDH 11, ALDH class 1, ALDH class 2, ALDH-E1, ALDH-E2, ALDHI, ALDM, ALHDII, ATP Binding Cassette Superfamily C Member 7, ATP binding cassette transporter sub family C member 7, ATP-binding cassette sub-family C member 7, Abacavir hypersensitivity, susceptibility to, Acetaldehyde dehydrogenase 1, Acetaldehyde dehydrogenase 2, Aldehyde dehydrogenase 1, Aldehyde dehydrogenase 1 family member A1, Aldehyde dehydrogenase 1 soluble, Aldehyde dehydrogenase 1A1, Aldehyde dehydrogenase 2 family, Aldehyde dehydrogenase 2 family (mitochondrial), Aldehyde dehydrogenase cytosolic, Aldehyde dehydrogenase liver cytosolic, Aldehyde dehydrogenase mitochondrial, Aldh, Antigen NY-CO-9, BCD541, BDMR, Beta-interferon, CD142, CD142 antigen, CDA07, CDLS5, CF, CFTR/MRP, CFTR_HUMAN, CPBHM, CTG 26, CTG repeat protein 26, Channel conductance-controlling ATPase, Coagulation factor III, Coagulation factor III (thromboplastin tissue factor), Component of gems 1, Cystic Fibrosis Transmembrane Regulator, Cystic fibrosis transmembrane conductance regulator, Cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub family C, member 7), Cystic fibrosis transmembrane conductance regulator ATP binding cassette sub family C member 7, D10Wsu179e, DKFZP586J0917, DKFZP761B039, DKFZp686H12203, Drug-induced liver injury due to flucloxacillin, EC 3.5.1.98, F3, FLJ16239, FLJ17960, FLJ22237, FLJ35621, FLJ37491, FLJ99588, Fibroblast interferon, GON 10, Gemin-1, HA6116, HD 10, HD 11, HD 2, HD 4, HD 6, HD 7, HD 7B, HD 7a, HD 8, HD 9, HD1, HD3, HD5, HDA10_HUMAN, HDA11_HUMAN, HDAC, HDAC 11, HDAC 7A, HDAC 7B, HDAC 9B, HDAC 9FL, HDAC A, HDAC1_HUMAN, HDAC2_HUMAN, HDAC3_HUMAN, HDAC4_HUMAN, HDAC5_HUMAN, HDAC6_HUMAN, HDAC7_HUMAN, HDAC8_HUMAN, HDAC9_HUMAN, HDACL-1, HDRP, HLA class I histocompatibility antigen, B-13 alpha chain, HLA class I histocompatibility antigen, B-14 alpha chain, HLA class I histocompatibility antigen, B-15 alpha chain, HLA class I histocompatibility antigen, B-18 alpha chain, HLA class I histocompatibility antigen, B-27 alpha chain, HLA class I histocompatibility antigen, B-35 alpha chain, HLA class I histocompatibility antigen, B-37 alpha chain, HLA class I histocompatibility antigen, B-38 alpha chain, HLA class I histocompatibility antigen, B-40 alpha chain, HLA class I histocompatibility antigen, B-41 alpha chain, HLA class I histocompatibility antigen, B-42 alpha chain, HLA class I histocompatibility antigen, B-44 alpha chain, HLA class I histocompatibility antigen, B-45 alpha chain, HLA class I histocompatibility antigen, B-46 alpha chain, HLA class I histocompatibility antigen, B-47 alpha chain, HLA class I histocompatibility antigen, B-48 alpha chain, HLA class I histocompatibility antigen, B-49 alpha chain, HLA class I histocompatibility antigen, B-50 alpha chain, HLA class I histocompatibility antigen, B-51 alpha chain, HLA class I histocompatibility antigen, B-52 alpha chain, HLA class I histocompatibility antigen, B-53 alpha chain, HLA class I histocompatibility antigen, B-54 alpha chain, HLA class I histocompatibility antigen, B-55 alpha chain, HLA class I histocompatibility antigen, B-56 alpha chain, HLA class I histocompatibility antigen, B-57 alpha chain, HLA class I histocompatibility antigen, B-58 alpha chain, HLA class I histocompatibility antigen, B-59 alpha chain, HLA class I histocompatibility antigen, B-67 alpha chain, HLA class I histocompatibility antigen, B-7 alpha chain, HLA class I histocompatibility antigen, B-73 alpha chain, HLA class I histocompatibility antigen, B-78 alpha chain, HLA class I histocompatibility antigen, B-8 alpha chain, HLA class I histocompatibility antigen, B-81 alpha chain, HLA class I histocompatibility antigen, B-82 alpha chain, Histone Deacetylase A, Histone deacetylase 1, Histone deacetylase 10, Histone deacetylase 11, Histone deacetylase 2, Histone deacetylase 2 (HD2), Histone deacetylase 3, Histone deacetylase 4, Histone deacetylase 4/5 related protein, Histone deacetylase 5, Histone deacetylase 6, Histone deacetylase 6 (HD6), Histone deacetylase 7, Histone deacetylase 7A, Histone deacetylase 7B, Histone deacetylase 8, Histone deacetylase 9, Histone deacetylase 9A, Histone deacetylase like 1, Histone deacetylase-related protein, IFB, IFF, IFN-beta, IFNB 1, IFNB_HUMAN, Interferon beta, Interferon beta 1 fibroblast, Interferon beta precursor, JM 21, KIAA0017, KIAA0288, KIAA0744, KIAA0901, KIAA1047, Liver mitochondrial ALDH, Lymphocyte antigen, MEF2 interacting transcription repressor protein, MEF2-interacting transcription repressor MITR, MGC149722, MGC1806, MGC2318, MGC96956, MHC class I antigen B 7, MITR, MRXS6, Major Histocompatibility Complex Class I B, Mitochondrial aldehyde dehydrogenase 2, Mono ADP ribosyltransferase sirtuin 6, N Cor/SMRT corepressor Rip13, N-CoR, NAD-dependent deacetylase sirtuin-2, NAD-dependent protein deacetylase sirtuin-2, NAD-dependent protein deacetylase sirtuin-6, NCOR1_HUMAN, NCOR2_HUMAN, NY CO 9, Nuclear Receptor Co-Repressor 2, Nuclear receptor corepressor 1, Nucleus encoded mitochondrial aldehyde dehydrogenase 2, OTTHUMP00000017046, OTTHUMP00000028555, OTTHUMP00000032398, OTTHUMP00000125198, OTTHUMP00000197663, OTTHUMP00000202813, OTTHUMP00000202814, OTTHUMP00000223567, OTTHUMP00000223568, OTTHUMP00000224066, OTTHUMP00000226924, OTTHUMP00000227077, OTTHUMP00000227078, PPP1R90, PUMB 1, Pre-mRNA-splicing factor SF3b 130 kDa subunit, Protein phosphatase 1 regulatory subunit 90, RALDH 1, RIP13, RPD 3, RPD3-2, RPD3L1, RSE1, Reduced potassium dependency yeast homolog like 1, Regulatory protein SIR2 homolog, Regulatory protein SIR2 homolog 2, Regulatory protein SIR2 homolog 6, Retinal dehydrogenase 1, Retinaldehyde dehydrogenase 1, Retinoid X receptor interacting protein 13, Rxrip13, SF3B3_HUMAN, SF3b130, SIR2 like 6, SIR2, S. cerevisiae, homolog-loke 2, SIR2-like protein 2, SIR2-like protein 6, SIR2L, SIR2L2, SIR2L6, SIR6_HUMAN, SIRT 2, SIRT2_HUMAN, SMA, SMA 1, SMA 2, SMA 3, SMA 4, SMAP 270, SMAP45, SMN1, SMN2, SMNT, SMN_HUMAN, SMRT, SMRTE, SMRTE tau, STAF130, Silencing Mediator for Retanoid and Thyroid Hormone Receptors, Silencing information regulator 2 like, Silencing mediator of retinoic acid and thyroid hormone receptor, Silent information regulator 2, Sir2 related protein type 2, Sir2 related protein type 6, Sirtuin (silent mating type information regulation 2 homolog) 2 (S.cerevisiae), Sirtuin (silent mating type information regulation 2 homolog) 6 (S. cerevisiae), Sirtuin 2, Sirtuin 6, Sirtuin type 2, Sirtuin type 6, Spliceosome-associated protein 130, Splicing factor 3B subunit 3, Splicing factor 3b subunit 3 130kD, Survival motor neuron protein, Survival of motor neuron 1, telomeric, Synovitis, chronic, susceptibility to, T-BCD541, T3 receptor-associating factor, TFA, TF_HUMAN, TNR CFTR, TNRC 14, TRAC 1, Thromboplastin, Thyroid retinoic acid receptor associated corepressor, Thyroid-, Tissue factor, WTS, YAF1, YY1 associated factor 1, YY1 transcription factor binding protein, Yy1bp, cAMP-dependent chloride channel, dJ760C5.1, hN CoR, leukocyte antigen class I-B, retinoic-acid-receptor-associated corepressor, thyroid hormone and retinoic acid receptor associated corepressor 1, transcriptional regulator homolog RPD3

2 Images
Chemical Structure - Trichostatin A, histone deacetylase inhibitor (AB120850)
  • Chemical Structure

Lab

Chemical Structure - Trichostatin A, histone deacetylase inhibitor (AB120850)

2D chemical structure image of ab120850, Trichostatin A, histone deacetylase inhibitor

Functional Studies - Trichostatin A, histone deacetylase inhibitor (AB120850)
  • FuncS

Unknown

Functional Studies - Trichostatin A, histone deacetylase inhibitor (AB120850)

Trichostatin A inhibits histone deacetylases in NIH/3T3 cells. Cells from logarithmic were incubated overnight with different concentrations of Trichostatin A (ab120850). Cell proteins were resolved by SDS-PAGE and probed with anti-acetylated histone antibodies.

Key facts

CAS number

58880-19-6

Purity

>98%

Form

Solid

form

Source

Streptomyces sp.

Molecular weight

302.37 Da

Molecular formula

C<sub>1</sub><sub>7</sub>H<sub>2</sub><sub>2</sub>N<sub>2</sub>O<sub>3</sub>

PubChem

444732

Nature

Native

Biochemical name

trichostatin A

Biological description

Potent, selective histone deacetylase (HDAC) inhibitor (Ki = 3.4 nM). Induces cell proliferation, differentiation and apoptosis in vitro. Anticancer and antifungal agent. Active in vivo and in vitro.

Canonical smiles

CC(C=C(C)C=CC(=O)NO)C(=O)C1=CC=C(C=C1)N(C)C

Isomeric smiles

C[C@H](/C=C(\C)/C=C/C(=O)NO)C(=O)C1=CC=C(C=C1)N(C)C

InChi

InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1

InChiKey

RTKIYFITIVXBLE-QEQCGCAPSA-N

IUPAC Name

(2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide

Properties and storage information

Shipped at conditions
Ambient - Can Ship with Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Store under desiccating conditions|The product can be stored for up to 12 months

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Histone deacetylases collectively known as HDACs include the enzymes HDAC1 HDAC2 HDAC3 HDAC4 HDAC5 HDAC6 HDAC7 HDAC8 HDAC9 HDAC10 and HDAC11. These proteins remove acetyl groups from histone proteins influencing chromatin structure and gene expression. HDAC1 for example has a molecular mass of approximately 55 kDa and is highly expressed in the nucleus of cells where it modifies chromatin architecture. The activity of these enzymes is tightly regulated and they often act as part of multi-subunit complexes to ensure precise control over transcription.
Biological function summary

HDACs play important roles in the regulation of gene expression by modifying the acetylation status of histones. They are integral parts of larger protein complexes such as the Sin3 complex or the NuRD complex which mediate interactions with chromatin to repress transcription. Through these complexes HDACs contribute to cell cycle regulation differentiation and apoptosis. The balance between acetylation and deacetylation maintained by HDACs and histone acetyltransferases (HATs) is critical for normal cellular function.

Pathways

These enzymes are essential in signaling and regulatory networks such as the Notch and p53 pathways. HDAC1 for instance interacts with the p53 protein to regulate cell cycle arrest and apoptosis. In the Notch signaling pathway HDACs participate in the regulation of cell fate determination. Their activity in these pathways often involves collaboration with other proteins including co-repressor proteins to exert their biological effects.

The dysregulation of HDAC activity has been associated with cancer and neurodegenerative diseases. In cancers such as leukemia aberrant HDAC1 activity can lead to uncontrolled cell proliferation due to the repression of tumor suppressor genes. In neurodegenerative conditions like Alzheimer's disease irregular HDAC6 function affects neuronal cell death and cognitive deficits. The therapeutic targeting of HDACs with inhibitors like SAHA (vorinostat) has shown promise in modulating these diseases highlighting the importance of HDACs as drug targets.

Product protocols

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Publications (5)

Recent publications for all applications. Explore the full list and refine your search

Animals : an open access journal from MDPI 15: PubMed40218304

2025

Preliminary Exploration of , , , and mRNA Expression in Canine Mammary Tumors in Dogs.

Applications

Unspecified application

Species

Unspecified reactive species

Wanwisa Srisawat,Pongpisid Koonyosying,Anucha Muenthaisong,Kanokwan Sangkakam,Thanya Varinrak,Nattawooti Sthitmatee

Anatomy & cell biology 58:247-263 PubMed39809587

2025

Liver oval cells in response to HDAC1 inhibitor trichostatin A: immunohistochemical characterization using OV-6 hepatic expression.

Applications

Unspecified application

Species

Unspecified reactive species

Hussein Abdellatif,Ruqaiya Al Jabri,Halima Albalushi,Mohamed Al Mushaiqri

Cell death & disease 13:466 PubMed35585040

2022

Macrophage migration inhibitory factor (MIF) acetylation protects neurons from ischemic injury.

Applications

Unspecified application

Species

Unspecified reactive species

Jin-Xia Hu,Wei-Jing Ma,Li-Ying He,Cong-Hui Zhang,Cheng Zhang,Yan Wang,Chao-Nan Chen,Da-Yong Shen,Hui-Min Gao,Rui-Ru Guo,Qian-Qian Ning,Xin-Chun Ye,Gui-Yun Cui,Lei Li

Molecular medicine reports 19:533-540 PubMed30483749

2018

Dexmedetomidine attenuates the toxicity of β‑amyloid on neurons and astrocytes by increasing BDNF production under the regulation of HDAC2 and HDAC5.

Applications

Unspecified application

Species

Unspecified reactive species

Yueling Wang,Aijun Jia,Wenjuan Ma

Learning & memory (Cold Spring Harbor, N.Y.) 23:195-207 PubMed27084927

2016

Involvement of phosphorylated Apis mellifera CREB in gating a honeybee's behavioral response to an external stimulus.

Applications

Unspecified application

Species

Unspecified reactive species

Katrin B Gehring,Karin Heufelder,Janina Feige,Paul Bauer,Yan Dyck,Lea Ehrhardt,Johannes Kühnemund,Anja Bergmann,Josefine Göbel,Marlene Isecke,Dorothea Eisenhardt
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