Size: | Price | Quantity | |
---|---|---|---|
5 mg | $65.00 | ||
25 mg | $260.00 |
Erastin (571203-78-6) is a ferroptosis inducer.1 Inhibits the cystine-glutamate antiporter, system Xc– leading to activation of an ER stress response.2 Inhibition of system Xc– leads to cysteine starvation, glutathione depletion and induction of ferroptosis.3 Also blocks mitochondrial voltage-dependent anion channels (specifically VDAC2 and 3).4
References/Citations:
1) Dolma et al. (2003), Identification of genotype-selective antitumor agents using synthetic lethal chemical screening in engineered human tumor cells; Cancer Cell, 3 285
2) Dixon et al. (2014), Pharmacological inhibition of cysteine-glutamate exchange induces endoplasmic reticulum stress and ferroptosis; Elife, 3 e02523
3) Sato et al. (2018), The ferroptosis inducer erastin irreversibly inhibits system xc-and synergizes with cisplatin to increase cisplatin’s cytotoxicity in cancer cells; Sci. Rep., 8 968
4) Yagoda et al. (2007), RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels; Nature, 447 864
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Erastin (571203-78-6) is a ferroptosis inducer.1 Inhibits the cystine-glutamate antiporter, system Xc– leading to activation of an ER stress response.2 Inhibition of system Xc– leads to cysteine starvation, glutathione depletion and induction of ferroptosis.3 Also blocks mitochondrial voltage-dependent anion channels (specifically VDAC2 and 3).4
References/Citations:
1) Dolma et al. (2003), Identification of genotype-selective antitumor agents using synthetic lethal chemical screening in engineered human tumor cells; Cancer Cell, 3 285
2) Dixon et al. (2014), Pharmacological inhibition of cysteine-glutamate exchange induces endoplasmic reticulum stress and ferroptosis; Elife, 3 e02523
3) Sato et al. (2018), The ferroptosis inducer erastin irreversibly inhibits system xc-and synergizes with cisplatin to increase cisplatin’s cytotoxicity in cancer cells; Sci. Rep., 8 968
4) Yagoda et al. (2007), RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels; Nature, 447 864
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