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HSP

Heat shock protein (HSP) inhibitors, mostly HSP90 inhibitors, block chaperones that fold and stabilize client proteins. HSP90 binds and hydrolyzes adenosine triphosphate (ATP), and many of its clients are kinases and transcription factors in growth signaling. In 1994, benzoquinone ansamycins such as geldanamycin were shown to disrupt HSP90 complexes with the viral Src kinase. A crystal structure reported in 1997 placed geldanamycin in the N-terminal ATP pocket of HSP90. Inhibition leads to degradation of client proteins through the ubiquitin-proteasome pathway. Later chemotypes include the resorcinol-based luminespib and ganetespib, alongside the geldanamycin analog alvespimycin hydrochloride. JG-98 is an allosteric inhibitor of HSP70, a second chaperone family.

1 Item

  • Liriodendrin
    Cat. No.
    A37531
    CAS No.
    573-44-4

    Liriodendrin

    Liriodendrin is a recognized agonist of Heat Shock Factor 1 (HSF1), a transcription factor crucial for the cellular stress response. Isolated from the plant E. ulmoides, Liriodendrin exhibits significant biological activity in regulating heat shock protein expression. This compound is valuable for research applications focusing on cellular protection, stress response mechanisms, and potential therapeutic strategies for diseases associated with protein misfolding.

    In stock View Details
    1 mg
    $350.00
    5 mg
    $895.00
    All 2 sizes

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