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AB141433

Tanespimycin (17-AAG), HSP90 inhibitor

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(5 Publications)

MW 585.7 Da, Purity >98%. Potent, selective HSP90 inhibitor (IC50 = 5 nM). Anticancer activity, including cytostatic, proapoptotic and antiangiogenic properties in vitro and in vivo.
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Chemical Structure - Tanespimycin (17-AAG), HSP90 inhibitor (AB141433)
  • Chemical Structure

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Chemical Structure - Tanespimycin (17-AAG), HSP90 inhibitor (AB141433)

2D chemical structure image of ab141433, Tanespimycin (17-AAG), HSP90 inhibitor

Key facts

CAS number

75747-14-7

Purity

>98%

Form

Solid

form

Molecular weight

585.7 Da

Molecular formula

C<sub>3</sub><sub>1</sub>H<sub>4</sub><sub>3</sub>N<sub>3</sub>O<sub>8</sub>

PubChem

6505803

Nature

Synthetic

Solubility

Soluble in DMSO to 100 mM

Soluble 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

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Complementary Products

Primary Antibodies

AB108252

Anti-ACE2 antibody [EPR4435(2)]

BOND RX™ Validated|RabMAb|Recombinant|KO Validated|20ul selling size

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-ACE2 antibody [EPR4435(2)] (AB108252)

  • 4
  • 10
Secondary Antibodies

AB150077

Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488)

Immunocytochemistry/ Immunofluorescence - Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488) (AB150077)

  • 5
  • 20
Primary Antibodies

AB203085

Anti-Hsp90 beta antibody [EPR16621]

20ul selling size|RabMAb|Recombinant|KO Validated

Flow Cytometry (Intracellular) - Anti-Hsp90 beta antibody [EPR16621] (AB203085)

  • 0
  • 0
Biochemicals

AB141248

Docetaxel, Cytotoxic agent

Chemical Structure - Docetaxel, Cytotoxic agent (AB141248)

  • 0
  • 0
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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
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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.
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Product protocols

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Publications (5)

Recent publications for all applications. Explore the full list and refine your search

Current protocols 4:e1038 PubMed38967962

2024

Ex Vivo Evaluation of the Function of Hematopoietic Stem Cells in Toxicology of Metals.

Applications

Unspecified application

Species

Unspecified reactive species

Jiaojiao Wu,Ting Liu,Mengke Tang,Yalin Liu,Wei Wang,Chuanxuan Wang,Yingzi Ju,Yifan Zhao,Yubin Zhang

Frontiers in cardiovascular medicine 9:842641 PubMed35402570

2022

Drug Screening Approach Using L1000-Based Connectivity Map and Its Application to COVID-19.

Applications

Unspecified application

Species

Unspecified reactive species

Takaharu Asano,Sarvesh Chelvanambi,Julius L Decano,Mary C Whelan,Elena Aikawa,Masanori Aikawa

Frontiers in oncology 10:624560 PubMed33569349

2021

A Novel Mechanism of 17-AAG Therapeutic Efficacy on HSP90 Inhibition in MYCN-Amplified Neuroblastoma Cells.

Applications

Unspecified application

Species

Unspecified reactive species

Reine Hanna,Jad Abdallah,Tamara Abou-Antoun

The Journal of biological chemistry 295:10138-10152 PubMed32385113

2020

Intramitochondrial proteostasis is directly coupled to α-synuclein and amyloid β1-42 pathologies.

Applications

Unspecified application

Species

Unspecified reactive species

Janin Lautenschläger,Sara Wagner-Valladolid,Amberley D Stephens,Ana Fernández-Villegas,Colin Hockings,Ajay Mishra,James D Manton,Marcus J Fantham,Meng Lu,Eric J Rees,Clemens F Kaminski,Gabriele S Kaminski Schierle

Journal of animal science 96:3358-3369 PubMed29800308

2018

Heat shock protein 90α couples with the MAPK-signaling pathway to determine meiotic maturation of porcine oocytes.

Applications

Unspecified application

Species

Unspecified reactive species

Yun-Hua Liu,Xiao-Man Liu,Pei-Chao Wang,Xiao-Xia Yu,Jia-Kun Miao,Shuai Liu,Yan-Kui Wang,Zhi-Qiang Du,Cai-Xia Yang
View all publications
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