HSF1A

Product NameHSF1A
CAS1196723-93-9
MFC21H19N3O2S2
MW409.52
EINECS
MOL File1196723-93-9.mol

Chemical Properties

Boiling point	592.6±60.0 °C(Predicted)
Density	1.31±0.1 g/cm3(Predicted)
storage temp.	Store at -20°C
solubility	DMSO:116.0(Max Conc. mg/mL);283.26(Max Conc. mM)
pka	6.53±0.10(Predicted)
form	Solid
color	White to off-white
InChI	1S/C21H19N3O2S2/c1-2-16-10-12-18(13-11-16)28(25,26)23-21-15-19(20-9-6-14-27-20)22-24(21)17-7-4-3-5-8-17/h3-15,23H,2H2,1H3
InChIKey	KJTITGSAONQVPY-UHFFFAOYSA-N
SMILES	[S](=O)(=O)(Nc2[n](nc(c2)c4[s]ccc4)c3ccccc3)c1ccc(cc1)CC

Safety Information

WGK Germany	WGK 3
Storage Class	11 - Combustible Solids

Usage And Synthesis

Uses

HSF1A is a cell-permeable activator of heat shock transcription factor 1 (HSF1)[1]. HSF1A also acts as a specific inhibitor of TRiC/CCT. Chaperonin TCP-1 ring complex (TRiC)/chaperonin containing TCP-1 (CCT) plays a pivotal role in toxin translocation and/or refolding[4].

Biological Activity

Cell permeable: yes', 'Primary Target
HSF1

in vivo

HSF1A enhances HSF1 activity, stabilizes HSF1 expression and minimizes Doxorubicin (DOX)-induced cardiac damage. WKY rats are challenged with DOX (accumulated dose: 30 mg/kgw), and DOX combined with HSF1A (100 mg/kgw/day). Supplementation with HSF1A significantly elevates cardiac functions back to the levels of the control group. HSF1A has been shown to stimulate human HSF1 nuclear translocation, elevate protein chaperone expression and ameliorate protein misfolding and cell death in a neurodegenerative disease model. The echocardiographic results show that HSF1A also alleviates DOX-induced failures in cardiac function^[3].

IC 50

HSF1

References

[1] Neef DW, et al. A direct regulatory interaction between chaperonin TRiC and stress-responsive transcription factor HSF1. Cell Rep. 2014 Nov 6;9(3):955-66. DOI:10.1016/j.celrep.2014.09.056
[2] Neef DW, et al. Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease. PLoS Biol. 2010 Jan 19;8(1):e1000291. DOI:10.1371/journal.pbio.1000291
[3] Huang CY, et al. Doxorubicin attenuates CHIP-guarded HSF1 nuclear translocation and protein stability to trigger IGF-IIR-dependent cardiomyocyte death. Cell Death Dis. 2016 Nov 3;7(11):e2455. DOI:10.1038/cddis.2016.356
[4] Marcus Steinemann, et al. The chaperonin TRiC/CCT is essential for the action of bacterial glycosylating protein toxins like Clostridium difficile toxins A and B. Proc Natl Acad Sci U S A. 2018 Sep 18;115(38):9580-9585. DOI:10.1073/pnas.1807658115

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