Key facts
CAS number:75747-14-7,
Purity:>98%,
Form:SolidSee storage information,
Molecular weight:585.7 Da,
Molecular formula:C31H43N3O8,
PubChem:6505803,
Nature:Synthetic,
Solubility:Soluble in DMSO to 100 mMSoluble in ethanol to 10 mM,
Biochemical name:Tanespimycin,
Biological description:Potent, selective HSP90 inhibitor (IC50 = 5 nM). Anticancer activity, including cytostatic, proapoptotic and antiangiogenic properties in vitro and in vivo.,
Canonical smiles:CC1CC(C(C(C=C(C(C(C=CC=C(C(=O)NC2=CC(=O)C(=C(C1)C2=O)NCC=C)C)OC)OC(=O)N)C)C)O)OC,
Isomeric smiles:C[C@H]1C[C@@H]([C@@H]([C@H](/C=C(/[C@@H]([C@H](/C=C\C=C(\C(=O)NC2=CC(=O)C(=C(C1)C2=O)NCC=C)/C)OC)OC(=O)N)\C)C)O)OC,
InChi:InChI=1S/C31H43N3O8/c1-8-12-33-26-21-13-17(2)14-25(41-7)27(36)19(4)15-20(5)29(42-31(32)39)24(40-6)11-9-10-18(3)30(38)34-22(28(21)37)16-23(26)35/h8-11,15-17,19,24-25,27,29,33,36H,1,12-14H2,2-7H3,(H2,32,39)(H,34,38)/b11-9-,18-10+,20-15+/t17-,19+,24+,25+,27-,29+/m1/s1,
InChiKey:AYUNIORJHRXIBJ-TXHRRWQRSA-N,
IUPAC Name:[(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-13-hydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3,20,22-trioxo-19-(prop-2-enylamino)-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl] carbamate
Properties and Storage Information:
Shipped at conditions-Ambient - Can Ship with Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information-Store under desiccating conditions
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Hsp90 also known as Heat Shock Protein 90 or Hsp90 beta plays an important role in protein folding and maintenance of cellular protein homeostasis. This molecular chaperone weighs approximately 90 kDa and is expressed in the cytosol of many different cell types. Hsp90 exists in two major isoforms Hsp90 alpha and Hsp90 beta which have similar functions but differ slightly in their expression across tissues with the beta form notably abundant in the liver.
Biological function summary
Hsp90 assists the maturation and stabilization of various client proteins many of which are important for the cell to respond to stress conditions. Hsp90 operates as part of a complex that includes co-chaperones and other regulatory proteins which fine-tune its chaperone activity. For instance ATP binding is essential for the structural changes in Hsp90 that enable it to hold its client proteins. The complex nature of Hsp90 enables its involvement in regulating proteins such as steroid hormone receptors and kinases among others.
Pathways
Research demonstrates the involvement of Hsp90 in important pathways like the signal transduction and protein folding pathways. In signal transduction Hsp90 interacts with kinases to stabilize them and ensure their proper function. Notably it is related to proteins like AAG and KOS953 as well as client proteins like the glucocorticoid receptor with whom it interacts during stress signal transduction processes. This makes Hsp90 a central player in cellular responses to environmental stimuli.
The involvement of Hsp90 in cancer and neurodegenerative diseases has been significant. Hsp90 stabilizes several oncoproteins making it a target in cancer treatments where its inhibitors are used to trigger the degradation of these proteins impacting cancer cell survival. Moreover disorders involving protein misfolding such as Alzheimer’s disease link to Hsp90 due to its fundamental role in protein homeostasis. Hsp90's interaction with disease-related proteins including mutated kinases and the amyloid precursor protein highlights its potential as a therapeutic target.
