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Heat shock proteins (HSPs) are a family of highly conserved proteins that are expressed, either constitutively or regulated inductively, in response to a wide range of physiological and environmental insults, such as heat shock. According to molecular weight, mammalian HSPs are classified into four subfamilies, including HSP90 (90 kDa), HSP70 (70 kDa), HSP60 (60 kDa) and small HSPs (15 to 30 kDa), among which HSP90 and HSP70 are two of the most studied stress-inducible HSPs. HSP90 is a highly abundant chaperone protein characterized by containing three relevant domains, including the N-terminal domain, the charged middle linker region and the C-terminal dimerization domain; while HSP70 is an ATP-dependent chaperone protein characterized by containing two distinct functional domains, including a peptide binding domain (PBD) and the amino-terminal ATPase domain (ABD). Collectively HSPs play a fundamental role in maintaining the stability of other cellular proteins.

Research Area

  1. Cat.No. Product Name Information
  2. A4054 17-AAG (KOS953) Hsp90 inhibitor
  3. A2213 17-DMAG (Alvespimycin) HCl Hsp90 inhibitor
  4. A4056 AT13387 Hsp90 inhibitor
  5. A4057 AUY922 (NVP-AUY922) Potent Hsp90 inhibitor
  6. A4058 BIIB021 Hsp90 inhibitor,selective and competitive
  7. B4920 EC 144 High affinity, potent and selective Hsp90 inhibitor
  8. A4386 Elesclomol (STA-4783) Oxidative stress/apoptosis inducer,potent and novel
  9. A4385 Ganetespib (STA-9090) Hsp90 inhibitor,non-geldanamycin
  10. B7393 Gedunin naturally occurring Hsp90 inhibitor
  11. A4060 Geldanamycin Hsp90 inhibitor,potent and specific

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