Compound 115-7c | HSP70 modulator
NMR (Conforms)
Available Options
| Size : | Price | Quantity | |
|---|---|---|---|
| 5 mg | $90.00 | ||
| 25 mg | $360.00 |
Compound 115-7c (908074-72-6) acts as an artificial co-chaperone for HSP70.1 The activity of compound 115-7c mirrors those of HSP40 stimulating the ATPase and protein-folding activities of prokaryotic HSP70. Increases tau levels in cell lines overexpressing tau.2 Induces solubilization of polyglutamine and exacerbates polyQ-mediated toxicity.3,4 Compound 115-7c is an important probe for understanding HSP70 functions.4
References/Citations:
1) Wisen et al. (2010), Binding of a small molecule at the protein-protein interface regulates the chaperone activity of hsp70-hsp40; ACS Chem. Biol., 5 611
2) Jinwal et al. (2010), Hsp70 ATPase Modulators as Therapeutics for Alzheimer’s and other Neurodegenerative Diseases; Mol. Cell Pharmacol., 2 43
3) Chafekar et al. (2012), Pharmacological tuning of heat shock protein 70 modulates polyglutamine toxicity and aggregation; ACS Chem. Biol., 7 1556
4) Walter et al. (2011), Ordered assembly of heat shock proteins Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probes; J. Biol. Chem., 286 40486
NMR (Conforms)
Safety Data Sheet:
Product Data Sheet:
Materials provided by Focus Biomolecules are for laboratory research use only and are not intended for human or veterinary applications. Please note that we do not sell to individuals and that all orders placed by non-research organizations will incur a $20 restocking/refund fee
Compound 115-7c (908074-72-6) acts as an artificial co-chaperone for HSP70.1 The activity of compound 115-7c mirrors those of HSP40 stimulating the ATPase and protein-folding activities of prokaryotic HSP70. Increases tau levels in cell lines overexpressing tau.2 Induces solubilization of polyglutamine and exacerbates polyQ-mediated toxicity.3,4 Compound 115-7c is an important probe for understanding HSP70 functions.4
References/Citations:
1) Wisen et al. (2010), Binding of a small molecule at the protein-protein interface regulates the chaperone activity of hsp70-hsp40; ACS Chem. Biol., 5 611
2) Jinwal et al. (2010), Hsp70 ATPase Modulators as Therapeutics for Alzheimer’s and other Neurodegenerative Diseases; Mol. Cell Pharmacol., 2 43
3) Chafekar et al. (2012), Pharmacological tuning of heat shock protein 70 modulates polyglutamine toxicity and aggregation; ACS Chem. Biol., 7 1556
4) Walter et al. (2011), Ordered assembly of heat shock proteins Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probes; J. Biol. Chem., 286 40486
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