An allosteric Hsp70 modulator
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YM-1 (trifluoroacetate salt)

Item No. 41174

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Formal Name
2-((3-ethyl-5-(3-methylbenzo[d]thiazol-2(3H)-ylidene)-4-oxothiazolidin-2-ylidene)methyl)-1-methylpyridin-1-ium, monotrifluoroacetate salt
Molecular Formula
C20H20N3OS2 • CF3COO
Formula Weight
495.5
Purity
≥98%
Formulation (Request formulation change)
A solid
Solubility(Learn about Variance in Solubility)
Ethanol: Slightly Soluble: 0.1-1 mg/ml
SMILES
O=C1C(SC(N1CC)=CC2=CC=CC=[N+]2C)=C3SC4=C(N3C)C=CC=C4.FC(C([O-])=O)(F)F
InChi Code
InChI=1S/C20H20N3OS2.C2HF3O2/c1-4-23-17(13-14-9-7-8-12-21(14)2)26-18(19(23)24)20-22(3)15-10-5-6-11-16(15)25-20;3-2(4,5)1(6)7/h5-13H,4H2,1-3H3;(H,6,7)/q+1;/p-1
InChi Key
YSPGKNZPFLRGOX-UHFFFAOYSA-M
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    1 mg

    $32

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    Cayman Chemical
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    Product Description

    YM-1 is an allosteric modulator of heat shock protein 70 (Hsp70).1 It binds to the Hsp70 N-terminal nucleotide-binding domain (NBD) and inhibits ATP/ADP turnover, thereby promoting substrate binding to the C-terminal substrate-binding domain (SBD). YM-1 (3 and 10 µM) reduces the viability of MCF-7 breast cancer cells. It induces degradation of the Hsp70 substrate protein bromodomain-containing protein 4 (BRD4), an effect that can be reversed by the proteasome inhibitor MG132 in MCF-7 cells. YM-1 (3 µM) lowers mutant huntingtin (mHTTQ74) levels and decreases the proportion of mHTTQ74 aggregates found in the nucleus over the cytoplasm in PC12 cells.2

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Mishima, Y., Tomoshige, S., Sato, S., et al. Allosteric Hsp70 modulator YM-1 induces degradation of BRD4. Chem. Pharm. Bull. (Tokyo) 72(2), 161-165 (2024).

    2. Pinho, B., Almeida, L.M., Duchen, M.R., et al. Allosteric activation of Hsp70 reduces mutant huntingtin levels, the clustering of N-terminal fragments, and their nuclear accumulation. Life Sci. 285, 120009 (2021).