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.
- Cat.No. Product Name Information
- A2213 17-DMAG (Alvespimycin) HCl 17-DMAG is an inhibitor of Hsp90 with IC50 value of 62±29nM .
- A3756 Retaspimycin Retaspimycin is a water-soluble hydroquinone hydrochloride salt inhibitor of Hsp90 .
- A3161 Alvespimycin Alvespimycin is a selective Hsp90 inhibitor with a GI50 of 53 nM.
- A4068 SNX-2112 SNX-2112 is a potent inhibitor of synthetic heat shock protein (Hsp 90) with IC50 value of 30 nM.
- A4065 PF-04929113 (SNX-5422) PF-04929113 is an inhibitor of Hsp90 .
- A4064 NVP-BEP800 NVP-BEP800 is a fully synthetic, orally bioavailable inhibitor of Hsp90 with IC50 value of 58nM .
- A4062 KW-2478 KW-2478 is a novel and potent nonansamycin inhibitor of heat shock protein 90 (Hsp90) to overcome the limitations, including low water solubility and hepatotoxicity, of 17-allylamino-17-demethoxygeldanamycin (17-AAG).
- A4061 IPI-504 (Retaspimycin hydrochloride) Retaspimycin hydrochloride (also known as IPI-504), a hydroquinone hydrochloride salt derivative of 17-AAG, is a novel, potent and selective inhibitor of heat shock protein 90(Hsp90) that binds to the amino-terminal ATP/ADP-binding site of Hsp90.
Geldanamycin, a crystalline antimicrobial compound derived from the culture filtrates of Streptomyces hygroscopicus var.
- A4058 BIIB021 BIIB021 is a selective inhibitor of Hsp90 with Ki and EC50 values of 1.7 nM and 38 nM, respectively.