Alvespimycin - CAS 467214-20-6
Not Intended for Therapeutic Use. For research use only.
Product Name:
Catalog Number:
17-DIMETHYLAMINOETHYLAMINO-17-DEMETHOXYG; 17-DMAGhydrochloride; 17-[2-(Dimethylamino)ethylamino]-17-desmethylgeldanamycin; 17-Demethoxy-17-[[2-(dimethylamino)ethyl]amino]geldanamycin; Alvespimycin; 17-DMAG (Alvespimycin)
CAS Number:
Alvespimycin (17-DMAG; KOS-1022; NSC 707545) is a potent, H2O-soluble Hsp90 inhibitor with IC50 of 62 nM.17-DMAG displays ~2 times potency against human Hsp90 than 17-AAG, with IC50 of 62 nM versus 119 nM. In SKBR3 and SKOV3 cells which over-express Hsp90 client protein Her2, 17-DMAG causes down-regulation of Her2 with EC50 of 8 nM and 46 nM, respectively, as well as induction of Hsp70 with EC50 of 4 nM and 14 nM, respectively, leading to significant cytotoxicity with GI50 of 29 nM and 32 nM, respectively, consistent with Hsp90 inhibition. 17-DMAG in combination with vorinostat synergistically induces apoptosis of the cultured MCL cells as well as primary MCL cells, more potently than either agent alone, by markedly attenuating the levels of cyclin D1 and CDK4, as well as of c-Myc, c-RAF and Akt. 17-DMAG treatment at 5 mg/kg or 25 mg/kg thrice per week significantly reduces tumor growth of TMK-1 xenografts, by significantly reducing vessel area and numbers of proliferating tumor cells in sections. Consistent the inhibition of FAK signaling in vivo, 17-DMAG treatment at 25 mg/kg three times a week significantly suppresses tumor growth, and metastasis of ME180 and SiHa xenografts in mice. Administration of 17-DMAG at 10 mg/kg for 16 days significantly decreases the white blood cell count and prolongs the survival in a TCL1-SCID transplant mouse model.
Molecular Weight:
Molecular Formula:
Quality Standard:
Canonical SMILES:
Hsp90 | HSP
Current Developer:
Chemical Structure
CAS 467214-20-6 Alvespimycin

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Reference Reading

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Iguchi N1, Malykhina AP1, Wilcox DT2. J Urol. 2016 Apr;195(4 Pt 2):1250-6. doi: 10.1016/j.juro.2015.08.001. Epub 2016 Feb 28.
PURPOSE: Posterior urethral valves are the most common cause of partial bladder outlet obstruction in the pediatric population. However, to our knowledge the etiology and the detailed mechanisms underlying pathological changes in the bladder following partial bladder outlet obstruction remain to be elucidated. Recent findings suggest that hypoxia and associated up-regulation of HIFs (hypoxia-inducible factors) have a key role in partial bladder outlet obstruction induced pathology in the bladder. We examined the effects of pharmacological inhibition of HIF pathways by 17-DMAG (17-(dimethylaminoethylamino)-17-demethoxygeldanamycin) in pathophysiological phenotypes after partial bladder outlet obstruction.
2.Targeting HSP90 Ameliorates Nephropathy and Atherosclerosis Through Suppression of NF-κB and STAT Signaling Pathways in Diabetic Mice.
Lazaro I1, Oguiza A2, Recio C2, Mallavia B1, Madrigal-Matute J3, Blanco J4, Egido J2, Martin-Ventura JL1, Gomez-Guerrero C5. Diabetes. 2015 Oct;64(10):3600-13. doi: 10.2337/db14-1926. Epub 2015 Jun 26.
Heat shock proteins (HSPs) are induced by cellular stress and function as molecular chaperones that regulate protein folding. Diabetes impairs the function/expression of many HSPs, including HSP70 and HSP90, key regulators of pathological mechanisms involved in diabetes complications. Therefore, we investigated whether pharmacological HSP90 inhibition ameliorates diabetes-associated renal damage and atheroprogression in a mouse model of combined hyperglycemia and hyperlipidemia (streptozotocin-induced diabetic apolipoprotein E-deficient mouse). Treatment of diabetic mice with 17-dimethylaminoethylamino-17-demethoxygeldanamycin (DMAG, 2 and 4 mg/kg, 10 weeks) improved renal function, as evidenced by dose-dependent decreases in albuminuria, renal lesions (mesangial expansion, leukocyte infiltration, and fibrosis), and expression of proinflammatory and profibrotic genes. Furthermore, DMAG significantly reduced atherosclerotic lesions and induced a more stable plaque phenotype, characterized by lower content of lipids, leukocytes, and inflammatory markers, and increased collagen and smooth muscle cell content.
3.Heat shock protein 90 inhibition by 17-Dimethylaminoethylamino-17-demethoxygeldanamycin protects blood-brain barrier integrity in cerebral ischemic stroke.
Qi J1, Liu Y1, Yang P1, Chen T1, Liu XZ1, Yin Y2, Zhang J1, Wang F3. Am J Transl Res. 2015 Oct 15;7(10):1826-37. eCollection 2015.
Metalloproteinase (MMP)9 plays a pivotal role in ischemic stroke induced blood brain barrier (BBB) disruption. Correlation between HSP90 and MMP9 in several diseases prompted us to evaluate the efficacy of HSP90 inhibition as a novel approach to protect BBB integrity in ischemic stroke. ELISA was used to detect HSP90α and MMP9 in serum samples of stroke patients, which showed that HSP90α significantly correlated with MMP9 among 63 serum samples of stroke patients. Male C57/BL6 mice were pretreated with 17-Dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) or vehicle before being subjected to transient occlusion of middle cerebral artery and reperfusion (MCAO). Infarction, neurological scores, Evans blue (EB) extravasation, inflammatory responses and tight junction protein expression were examined 24 h after MCAO. We also investigated if 17-DMAG protected BBB integrity by suppressing inflammation and MMP9 activation. Oxygen glucose deprivation (OGD) was performed on bEnd.
4.Heat shock protein 90 inhibitor regulates necroptotic cell death via down-regulation of receptor interacting proteins.
Park SY, Shim JH, Chae JI, Cho YS. Pharmazie. 2015 Mar;70(3):193-8.
17-(Dimethylaminoethylamino)-17-demethoxygeldanamycin (DMAG) acts as an inhibitor of heat shock protein 90 (HSP 90), which serves as a nodal protein of diverse signaling networks leading to a variety of biological implications. HSP90 plays the role of a chaperone for a variety of client proteins including receptor interacting protein 1 (RIP1). Since RIP1 and RIP3 are, respectively, required for zVAD- and tumor necrosis factor alpha (TNFα)-mediated necrotic cell death, we pursued to address the effects of DMAG on receptor-and nonreceptor-mediated necroptotic cell death. DMAG facilitated the degradation of receptor interacting protein 3 (RIP3) as well as RIP1, a known client protein of HSP90, in L929 cells. Consequently, DMAG rendered cells more sensitive to TNFα stimulation while it rescued cells from necrotic cell death caused by zVAD. From this study, we propose that DMAG-downregulated RIP1 can shift cell death typing from necroptosis to apoptosis.