Name: 17-AAG (KOS953)
Price: 212.00 USD

- Overview
  - Please contact us at for specific academic pricing.
    
    Background
    
    17-AAG is a potent inhibitor of HSP90 with IC50 value of 6 nM in BT474 cells [1].
    17-AAG is a synthetic analogue developed from geldanamycin which was found to have significant hepatic toxicity. 17-AAG has an improved toxicity profile and has no hepatic toxicity. 17-AAG can bind to HSP90 and destabilize the client proteins such as HER2, Raf-1, p53 and MAPK signaling. In Multiple myeloma (MM) cells, 17-AAG treatment inhibited cell proliferation and survival. The combination treatment of 17-AAG and bortezomib induced apoptosis in primary MM cells resistant to doxorubicin and bortezomib. The combination of 17-AAG and trastuzumab reduced the expression of ErbB2 in breast cancer cells overexpressing ErbB2. 17-AAG also showed efficacy in thyroid cancer cells and Hodgkin lymphoma cells. Besides that, 17-AAG was found to increased apoptosis in human melanoma xenografts. 17-AAG is now in phase II clinical studies [2].
    
    [1] Kamal A, Thao L, Sensintaffar J, et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors[J]. Nature, 2003, 425(6956): 407-410..
    [2] Dimopoulos M A, Mitsiades C S, Anderson K C, et al. Tanespimycin as antitumor therapy. Clinical Lymphoma Myeloma and Leukemia, 2011, 11(1): 17-22
- Properties
  - Alternative Name
    
    Tanespimycin; [(3R,5S,6R,7S,8E,10S,11S,12Z,14E)-6-hydroxy-5,11-dimethoxy-3,7,9,15-tetramethyl-16,20,22-trioxo-21-(prop-2-enylamino)-17-azabicyclo[16.3.1]docosa-1(21),8,12,14,18-pentaen-10-yl] carbamate
    
    CAS Number
    
    75747-14-7
    
    Molecular Formula
    
    C31H43N3O8
    
    Molecular Weight
    
    585.7
    
    Appearance
    
    A solid
    
    Purity
    
    98.00%
    
    Solubility
    
    ≥24.95 mg/mL in DMSO; insoluble in H2O; ≥9.56 mg/mL in EtOH with ultrasonic
    
    Storage
    
    Store at -20°C
    
    * For Research Use Only
- Reference
  - 1. Yixuan Wang, Quan Chen, et al. "Lamin-A interacting protein Hsp90 is required for DNA damage repair and chemoresistance of ovarian cancer cells." Cell Death Dis. 2021 Aug 12;12(8):786. PMID:34381017
    2. Diwei Zheng, Weihai Liu, et al. "AHA1 upregulates IDH1 and metabolic activity to promote growth and metastasis and predicts prognosis in osteosarcoma." Signal Transduct Target Ther. 2021 Jan 20;6(1):25. PMID:33468990
    3. Liam Baird, Takafumi Suzuki, et al. "Geldanamycin-derived HSP90 Inhibitors are Synthetic Lethal with NRF2." Mol Cell Biol 2020 Aug 31;MCB.00377-20. PMID:32868290
    4. Zora Chui-Kuen Chan, Linyan Deng, et al. "Grp94 regulates the recruitment of aneural AChR clusters for the assembly of postsynaptic specializations by modulating ADF/cofilin activity and turnover." eNeuro 3 August 2020, ENEURO.0025-20.2020. PMID:32747457
    5. Bi Liu, Yunzhu Shen, et al. "Curcumin Derivative C212 Inhibits Hsp90 and Eliminates Both Quiescent and Growing Leukemia Cells." Preprints.org. 17 November 2019.
    6. Karney-Grobe S, Russo A, et al. "HSP90 is a chaperone for DLK and is required for axon injury signaling." Proc Natl Acad Sci U S A. 2018 Oct 16;115(42):E9899-E9908. PMID:30275300
    7. Jarrett Smith,Geraldine Seydoux, et al. "Liquid-like P granules require ATP hydrolysis to avoid solidification." bioRxiv,Jan. 10, 2018.
    8. Khattar, Vinayak, et al. "Cks1 proteasomal degradation is induced by inhibiting Hsp90-mediated chaperoning in cancer cells." Cancer chemotherapy and pharmacology (2014): 1-10. PMID:25544127

17-AAG (KOS953)

17-AAG (KOS953)

Background

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