| Identification | Back Directory | [Name]
HSF1A | [CAS]
1196723-93-9 | [Synonyms]
HSF1A
HSF1 Activator
CAS 1196723-93-9
HSF1 ACTIVATOR;HSF1A;CAS 1196723-93-9
Benzenesulfonamide, 4-ethyl-N-[1-phenyl-3-(2-thienyl)-1H-pyrazol-5-yl]- | [Molecular Formula]
C21H19N3O2S2 | [MDL Number]
MFCD22580417 | [MOL File]
1196723-93-9.mol | [Molecular Weight]
409.52 |
| Chemical Properties | Back Directory | [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) | [form ]
Solid | [pka]
6.53±0.10(Predicted) | [color ]
White to off-white |
| Hazard Information | Back Directory | [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 | [storage]
Store at -20°C | [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 |
|
|