Ricolinostat (ACY-1215)

Catalog No.S8001 Synonyms: Rocilinostat

Ricolinostat (ACY-1215)  Chemical Structure

Molecular Weight(MW): 433.5

Ricolinostat (ACY-1215) is a selective HDAC6 inhibitor with IC50 of 5 nM in a cell-free assay. It is >10-fold more selective for HDAC6 than HDAC1/2/3 (class I HDACs) with slight activity against HDAC8, minimal activity against HDAC4/5/7/9/11, Sirtuin1, and Sirtuin2. Phase 2.

Size Price Stock Quantity  
In DMSO USD 190 In stock
USD 110 In stock
USD 170 In stock
USD 570 In stock
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3 Customer Reviews

  • (a) Representative images from hTERT RPE-1 cells transiently transfected with siControl (siC), treated with vehicle (DMSO), alisertib (MLN8237) or rocilinostat (ACY1215) at the time of serum withdrawal for 48 h. Ciliation monitored by immunofluorescent staining using acetylated α-tubulin (cilia marker) and pericentrin (basal body marker). Nuclei counterstained using DAPI. Highlighted boxes show magnified cilia. Scale bar, 3 μM.

    Oncogene, 2017. Ricolinostat (ACY-1215) purchased from Selleck.

    Immunoblot of MB99-1 cells treated with the indicated compound concentrations for 48 hours. Note that the HDAC6-selective inhibitors affect tubulin acetylation, but not histone H3 acetylation, whereas the pan-HDAC inhibitor TSA increases the acetylation of both.

    Mol Cancer Ther, 2015, 14(3):727-39.. Ricolinostat (ACY-1215) purchased from Selleck.

  • E. The expression levels of TP and TS mRNA were evaluated by qRealTime-PCR in untreated MCF-7 cells and in MCF-7 cells that were untreated or treated with selective HDACi at the indicated concentrations for 24 hours. F. The expression of TP, TS, acetylated H3 and acetylated α-tubulin proteins was determined by western blot in untreated cells and in MCF-7 cells that were treated for 48 hours with different HDACi at the indicated concentrations. α-tubulin was used as the protein loading control

    Oncotarget, 2016, 7(7):7715-31. Ricolinostat (ACY-1215) purchased from Selleck.

Purity & Quality Control

Choose Selective HDAC Inhibitors

Biological Activity

Description Ricolinostat (ACY-1215) is a selective HDAC6 inhibitor with IC50 of 5 nM in a cell-free assay. It is >10-fold more selective for HDAC6 than HDAC1/2/3 (class I HDACs) with slight activity against HDAC8, minimal activity against HDAC4/5/7/9/11, Sirtuin1, and Sirtuin2. Phase 2.
Features Induced less cytotoxicity in PHA-stimulated PBMCs from 4 healthy donors compared with the pan-HDAC inhibitor SAHA.
HDAC6 [1]
(Cell-free assay)
HDAC2 [1]
(Cell-free assay)
HDAC3 [1]
(Cell-free assay)
HDAC1 [1]
(Cell-free assay)
HDAC8 [1]
(Cell-free assay)
4.7 nM 48 nM 51 nM 58 nM 100 nM
In vitro

ACY-1215 is a hydroxamic acid derivative. ACY-1215 is 12-, 10-, and 11-fold less active against HDAC1, HDAC2, and HDAC3 (class I HDACs), respectively. ACY-1215 has minimal activity (IC50 > 1μM) against HDAC4, HDAC5, HDAC7, HDAC9, HDAC11, Sirtuin1, and Sirtuin2, and has slight activity against HDAC8 (IC50 = 0.1μM). The IC50 values for ACY-1215 for T-cell toxicity is 2.5μM. ACY-1215 overcomes tumor cell growth and survival conferred by BMSCs and cytokines in the BM milieu. ACY-1215 in combination with bortezomib induces synergistic anti-MM activity. ACY-1215 induces potent acetylation of α-tubulin at very low doses and triggers acetylation of lysine on histone H3 and histone H4 only at higher doses, confirming its specific inhibitory effect on HDAC6 activity. [1]

Cell Data
Cell Lines Assay Type Concentration Incubation Time Formulation Activity Description PMID
RPMI8226 NHSwNohIem:5dHigTY5pcWKrdHnvckBCe3OjeR?= MXPJR|UxRTF2NkigxtEhOzFyIH7N MlnaNlY1PDNyN{i=
A-172 Mn;aS5Jwf3SqIFnubIljcXSrb36gRZN{[Xl? NV63WXpxOTEEoH7N M1q1N|I1NzR6IHi= NGrLZ41qdmirYnn0d{Bk\WyuIHfyc5d1cCC2aX3lJIRmeGWwZHXueIx6 M1vwT|I3OTVyM{Sw
U87MG M{[5cWdzd3e2aDDJcohq[mm2aX;uJGF{e2G7 NYDzUmo4OTEEoH7N MoTYNlQwPDhiaB?= Mmn5bY5pcWKrdIOgZ4VtdCCpcn;3eIghfGmvZTDk[ZBmdmSnboTsfS=> M1P3e|I3OTVyM{Sw
Hbl-1 MXrHdo94fGhiSX7obYJqfGmxbjDBd5NigQ>? MnvWOFghcA>? M{\JUmlEPTB;MT62JO69VQ>? NFflW3gzPjFzNkK3NC=>
OCI-Ly10 M2rzSmdzd3e2aDDJcohq[mm2aX;uJGF{e2G7 NEDT[Gk1QCCq NFHxRo5KSzVyPUCuPUDPxE1? M2TqXlI3OTF4Mkew
Riva NX3JWohtT3Kxd4ToJGlvcGmkaYTpc44hSXO|YYm= NY\IPFh5PDhiaB?= M374fmlEPTB;Mj6yJO69VQ>? MmTBNlYyOTZ{N{C=
OCI-Ly1 MoP4S5Jwf3SqIFnubIljcXSrb36gRZN{[Xl? NGLhNm81QCCq NXXlbZg5UUN3ME2yMlQh|ryP NHHyXYYzPjFzNkK3NC=>
OCI-Ly7 MUTHdo94fGhiSX7obYJqfGmxbjDBd5NigQ>? MnfrOFghcA>? M3X5cGlEPTB;MT6yJO69VQ>? NHfkdoYzPjFzNkK3NC=>
Su-DHL4 NUXZdnBFT3Kxd4ToJGlvcGmkaYTpc44hSXO|YYm= MlLvOFghcA>? MXjJR|UxRTRwNzFOwG0> MlT2NlYyOTZ{N{C=
Su-DHL6 MXHHdo94fGhiSX7obYJqfGmxbjDBd5NigQ>? NEW0b3o1QCCq MoPlTWM2OD1|LkKg{txO NID1PVUzPjFzNkK3NC=>
Hbl-2 NHXaW4ZIem:5dHigTY5pcWKrdHnvckBCe3OjeR?= NYPwenJ2PDhiaB?= NYDWPXRIUUN3ME2xMlkh|ryP MofuNlYyOTZ{N{C=
Jeko-1 NEKybWZIem:5dHigTY5pcWKrdHnvckBCe3OjeR?= NUD4XVFEPDhiaB?= NGrmb3NKSzVyPUGuOUDPxE1? NWCxUVZyOjZzMU[yO|A>
Jvm-2 MVjHdo94fGhiSX7obYJqfGmxbjDBd5NigQ>? MX20PEBp M4LBemlEPTB;ND6wJO69VQ>? NUP0WJBkOjZzMU[yO|A>
Rec-1  MVzHdo94fGhiSX7obYJqfGmxbjDBd5NigQ>? MUC0PEBp M1rVcmlEPTB;Mj6zJO69VQ>? MVeyOlEyPjJ5MB?=
CCL-119 MWHHdo94fGhiSX7obYJqfGmxbjDBd5NigQ>? M2fqdFQ5KGh? MXvJR|UxRTFwNzFOwG0> NX7aPJpbOjZzMU[yO|A>
H9 NGXv[HpIem:5dHigTY5pcWKrdHnvckBCe3OjeR?= Mn7UOFghcA>? M1HDfWlEPTB;MT6yJO69VQ>? Mlv6NlYyOTZ{N{C=
HH MkDYS5Jwf3SqIFnubIljcXSrb36gRZN{[Xl? MnfDOFghcA>? MVvJR|UxRTJwNTFOwG0> NIPQe4ozPjFzNkK3NC=>
Sup-T1 MVvHdo94fGhiSX7obYJqfGmxbjDBd5NigQ>? NVKwUmMxPDhiaB?= M37VNmlEPTB;MT62JO69VQ>? MWGyOlEyPjJ5MB?=
MM.1S MWrGeY5kfGmxbjDBd5NigQ>? NGPS[G4xNTYQvF2= MXS2JIg> NXvoT3FzcW6lcnXhd4V{KGGlZYT5cIF1\WRizsGteJVjfWyrbh?= MkDuNlIzPjJ5NkC=
MM.1S NHjVWGhHfW6ldHnvckBCe3OjeR?= NUfUSZBiOC5{NT:x{txO NHzKZ4syQCCq M1fFOYlv[3KnYYPld{Bi[2W2eXzheIVlKM7zLYT1ZpVtcW5? NFHqe4wzOjJ4Mke2NC=>
MM.1R NVvhTFhxTnWwY4Tpc44hSXO|YYm= M{jiN|AvOjVxMd88US=> M2XnOFE5KGh? MUjpcoNz\WG|ZYOgZYNmfHmuYYTl[EDPuS22dXL1cIlv Mn70NlIzPjJ5NkC=
RPMI8226  NVfYOpR5TnWwY4Tpc44hSXO|YYm= MYmwMlI2NzIQvF2= NHrEfIkyQCCq MWLpcoNz\WG|ZYOgZYNmfHmuYYTl[EDPuS22dXL1cIlv MoHtNlIzPjJ5NkC=
MM.1S MUDD[YxtKF[rYXLpcIl1gSCDc4PhfS=> NGrQUlYxNTkQvF2= Mlz3OFghcA>? MYDk[YNz\WG|ZYOgUW0u[2WubDD2bYFjcWyrdImgbY4h[SCmb4PlMYRmeGWwZHXueEBu[W6wZYK= M17PSFIzOjZ{N{[w
OPM1 NVriNoI2S2WubDDWbYFjcWyrdImgRZN{[Xl? NFfDO4YxNTkQvF2= NILlT3c1QCCq M1jJdYRm[3KnYYPld{BOVS2lZXzsJJZq[WKrbHn0fUBqdiCjIHTvd4Uu\GWyZX7k[Y51KG2jbn7ldi=> NYjPUIRWOjJ{NkK3OlA>
RPMI NUHOPXpSS2WubDDWbYFjcWyrdImgRZN{[Xl? NH\JSHMxNTkQvF2= M1;WdFQ5KGh? MnjS[IVkemWjc3XzJG1ONWOnbHygeoli[mmuaYT5JIlvKGFiZH;z[U1l\XCnbnTlcpQhdWGwbnXy NX\ndVJlOjJ{NkK3OlA>
MM.1R MWDD[YxtKF[rYXLpcIl1gSCDc4PhfS=> Ml7XNE05|ryP NH3GSnQ1QCCq Mlfw[IVkemWjc3XzJG1ONWOnbHygeoli[mmuaYT5JIlvKGFiZH;z[U1l\XCnbnTlcpQhdWGwbnXy NIP0emczOjJ4Mke2NC=>
LR5 M1jucGNmdGxiVnnhZoltcXS7IFHzd4F6 MnjTNE05|ryP NI\rUFc1QCCq MWjk[YNz\WG|ZYOgUW0u[2WubDD2bYFjcWyrdImgbY4h[SCmb4PlMYRmeGWwZHXueEBu[W6wZYK= MojuNlIzPjJ5NkC=
OPM2 MkHiR4VtdCCYaXHibYxqfHliQYPzZZk> MorWNE05|ryP MkjiOFghcA>? NInCcXhl\WO{ZXHz[ZMhVU1vY3XscEB3cWGkaXzpeJkhcW5iYTDkc5NmNWSncHXu[IVvfCCvYX7u[ZI> M4fpe|IzOjZ{N{[w

... Click to View More Cell Line Experimental Data

In vivo ACY-1215 in combination with bortezomib triggered more significant anti-MM activity than either agent alone in suppressing tumor growth and prolonging survival in both plasmacytoma model and disseminated MM model without significant adverse effects. ACY-1215 is readily absorbed by tumor tissue. Moreover, the drug does not accumulate in tumor tissue, as evidenced by the parallel decline of acetylated α-tubulin in blood cells and tumor tissue by 24 hours after dose. [1]


Kinase Assay:


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HDAC enzymatic assays:

ACY-1215 is dissolved and subsequently diluted in assay buffer [50 mM HEPES, pH 7.4, 100 mM KCl, 0.001% Tween-20, 0.05% BSA, and 20 μM tris(2-carboxyethyl)phosphine] to 6-fold the final concentration. HDAC enzymes are diluted to 1.5-fold of the final concentration in assay buffer and pre-incubated with ACY-1215 for 10 minutes before the addition of the substrate. The amount of FTS (HDAC1, HDAC2, HDAC3, and HDAC6) or MAZ-1675 (HDAC4, HDAC5, HDAC7, HDAC8, and HDAC9) used for each enzyme is equal to the Michaelis constant (Km), as determined by a titration curve. FTS or MAZ-1675 is diluted in assay buffer to 6-fold the final concentration with 0.3μM sequencing grade trypsin. The substrate/trypsin mix is added to the enzyme/compound mix and the plate is shaken for 60 seconds and then placed into a SpectraMax M5 microtiter plate reader. The enzymatic reaction is monitored for release of 7-amino-4-methoxy-coumarin over 30 minutes, after deacetylation of the lysine side chain in the peptide substrate, and the linear rate of the reaction is calculated.
Cell Research:


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  • Cell lines: MM cell lines, patient MM cells, and PBMCs
  • Concentrations: ~8 μM
  • Incubation Time: 48 hours
  • Method:

    PBMCs from healthy donors are isolated and stimulated with 2.5 μg/mL of phytohemagglutinin (PHA) for 48 hours in the presence of increasing concentrations of ACY-1215. DNA synthesis is measured by tritiated thymidine uptake. CD4+T cells are purified from human blood with the Rosette Sep negative-selection kit. Cells are stimulated by CD3/CD28 Dynabeads for 7 days in the presence of compounds. Cell viability is assessed using alamarBlue. MM cells (2-3 × 104cells/well) are incubated in 96-well culture plates with medium and different concentrations of ACY-1215, bortezomib, and/or recombinant IL-6 (10 ng/mL) or insulin-like growth factor-1 (IGF-1; 50 ng/mL) for 24 hours at 37°C, and tritiated thymidine incorporation is measured.

    (Only for Reference)
Animal Research:


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  • Animal Models: MM xenograft SCID mouse model
  • Formulation: 10% DMSO in 5% dextrose in water
  • Dosages: 50 mg/kg
  • Administration: ip
    (Only for Reference)

Solubility (25°C)

In vitro DMSO 86 mg/mL (198.38 mM)
Water Insoluble
Ethanol Insoluble
In vivo Add solvents individually and in order:
2% DMSO+30% PEG 300+ddH2O

* Please note that Selleck tests the solubility of all compounds in-house, and the actual solubility may differ slightly from published values. This is normal and is due to slight batch-to-batch variations.

Chemical Information

Molecular Weight 433.5


CAS No. 1316214-52-4
Storage powder
Synonyms Rocilinostat

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Clinical Trial Information

NCT Number Recruitment Conditions Sponsor/Collaborators Start Date Phases
NCT02787369 Recruiting Recurrent Chronic Lymphoid Leukemia Dana-Farber Cancer Institute|Acetylon Pharmaceuticals Incorporated May 2016 Phase 1
NCT02632071 Recruiting Metastatic Breast Cancer|Breast Carcinoma Kevin Kalinsky|Acetylon Pharmaceuticals Incorporated|Columbia University February 2016 Phase 1
NCT02189343 Active, not recruiting Multiple Myeloma Acetylon Pharmaceuticals Incorporated August 2014 Phase 1
NCT02091063 Recruiting Lymphoma|Lymphoid Malignancies Jennifer Amengual|Acetylon Pharmaceuticals Incorporated|Columbia University March 2014 Phase 1|Phase 2
NCT02088398 Completed Healthy Acetylon Pharmaceuticals Incorporated March 2014 Phase 1
NCT01997840 Active, not recruiting Multiple Myeloma Acetylon Pharmaceuticals Incorporated November 2013 Phase 1|Phase 2

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Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

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Frequently Asked Questions

  • Question 1:

    What would you suggest to obtain a clear solution?

  • Answer:

    S8001 ACY-1215 can be dissolved in 2% DMSO/30% PEG 300/ddH2O at 5 mg/ml clearly while it in 1% DMSO/30% polyethylene glycol/1% Tween 80 at 30 mg/ml is a suspension for oral administration. Please note that the precipitation will go out from the clear solution after stayed for about half an hour, So it is recommended to prepare the solution just before use.

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Cell Lines Assay Type Concentration Incubation Time Formulation Activity Description PMID