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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.

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  • HSP70/DnaK substrate peptide
    Cat. No.
    A37555
    CAS No.
    156343-40-7

    HSP70/DnaK substrate peptide

    HSP70/DnaK substrate peptide is a specific peptide recognized and bound by the HSP70/DnaK molecular chaperone. This substrate peptide is essential for probing the functional mechanisms of HSP70/DnaK, facilitating the investigation of its role in protein folding, stabilization, and stress response pathways. It serves as a valuable tool for research applications focused on understanding molecular chaperone activity and cellular proteostasis.

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