HSF1A is an activator of Heat shock transcription factor 1 (HSF1). HSF1A protects cells from stress-induced apoptosis, binds TRiC subunits and inhibits TRiC activity without perturbation of ATP hydrolysis. HSF1A enhances HSF1 activity, stabilizes HSF1 expression and minimizes Doxorubicin (DOX)-induced cardiac damage. 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.
|Body Surface Area (m2)||0.007||0.025||0.15||0.05||0.02||0.5|
|Animal A (mg/kg) = Animal B (mg/kg) multiplied by||Animal B Km|
|Animal A Km|
For example, to modify the dose of resveratrol used for a mouse (22.4 mg/kg) to a dose based on the BSA for a rat, multiply 22.4 mg/kg by the Km factor for a mouse and then divide by the Km factor for a rat. This calculation results in a rat equivalent dose for resveratrol of 11.2 mg/kg.
|Solubility||DMSO: ≥ 90 mg/mL|
Doxorubicin attenuates CHIP-guarded HSF1 nuclear translocation and protein stability to trigger IGF-IIR-dependent cardiomyocyte death.
Huang CY, et al. Cell Death Dis. 2016 Nov 3;7(11):e2455. PMID: 27809308.
A direct regulatory interaction between chaperonin TRiC and stress-responsive transcription factor HSF1.
Neef DW, et al. Cell Rep. 2014 Nov 6;9(3):955-66. PMID: 25437552.
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