Novel adenosine-derived inhibitor of Heat Shock Protein 70 (Hsp70) (IC50 = 0.5 μM). Inhibits cell proliferation of multiple human tumor cell lines in vitro. Also binds Hsc70 and Grp78; displays selectivity against Hsp90β (IC50 >200 μM for Hsp90β).
|Storage||Desiccate at RT|
The technical data provided above is for guidance only. For batch specific data refer to the Certificate of Analysis.
All Tocris products are intended for laboratory research use only.
|Solvent||Max Conc. mg/mL||Max Conc. mM|
Preparing Stock Solutions
The following data is based on the product molecular weight 556.4. Batch specific molecular weights may vary from batch to batch due to solvent of hydration, which will affect the solvent volumes required to prepare stock solutions.
|Concentration / Solvent Volume / Mass||1 mg||5 mg||10 mg|
|1 mM||1.8 mL||8.99 mL||17.97 mL|
|5 mM||0.36 mL||1.8 mL||3.59 mL|
|10 mM||0.18 mL||0.9 mL||1.8 mL|
|50 mM||0.04 mL||0.18 mL||0.36 mL|
References are publications that support the biological activity of the product.
Massey et al (2009) A novel, small molecule inhibitor of Hsc70/Hsp70 potentiates Hsp90 inhibitor induced apoptosis in HCT116 colon carcinoma cells. Cancer Chemother.Pharmacol. 66 535 PMID: 20012863
Williamson et al (2009) Novel adenosine-derived inhibitors of 70 kDa heat shock protein, discovered through structure-based design. J.Med.Chem. 52 1510 PMID: 19256508
Massey et al (2010) ATPases as drug targets: insights from heat shock proteins 70 and 90. J.Med.Chem. 53 7280 PMID: 20608738
Macias et al (2011) Adenosine-derived inhibitors of 78 kDa glucose regulated protein (Grp78) ATPase: insights into isoform selectivity. J.Med.Chem. 54 4034 PMID: 21526763
If you know of a relevant reference for VER 155008, please let us know.
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Keywords: VER 155008, VER 155008 supplier, VER155008, HSP, 70, antagonist, HSP70, adenosine, derived, inhibitor, inhibitors, inhibits, heat, shock, protein, selective, Hsp90, Hsp70, 3803, Tocris Bioscience
13 Citations for VER 155008
Citations are publications that use Tocris products. Selected citations for VER 155008 include:
Young et al (2015) A novel mechanism of autophagic cell death in dystrophic muscle regulated by P2RX7 receptor large-pore formation and HSP90. Oncotarget 11 113 PMID: 25700737
Thuringer et al (2015) Oncogenic extracellular HSP70 disrupts the gap-junctional coupling between capillary cells. J Cell Biol 6 10267 PMID: 25868858
O'Regan et al (2015) Hsp72 is targeted to the mitotic spindle by Nek6 to promote K-fiber assembly and mitotic progression. J Biol Chem 209 349 PMID: 25940345
Couceiro et al (2015) Sequence-dependent internalization of aggregating peptides. Retrovirology 290 242 PMID: 25391649
Truman et al (2015) Quantitative proteomics of the yeast Hsp70/Hsp90 interactomes during DNA damage reveal chaperone-dependent regulation of ribonucleotide reductase. J Proteomics 112 285 PMID: 25452130
Baquero-Perez and Whitehouse (2015) Hsp70 Isoforms Are Essential for the Formation of Kaposi's Sarcoma-Associated Herpesvirus Replication and Transcription Compartments. PLoS Pathog 11 e1005274 PMID: 26587836
Nair et al (2015) The regulation of TNFα production after heat and endotoxin stimulation is dependent on Annexin-A1 and HSP70. Cell Stress Chaperones 20 583 PMID: 25753354
Rodriguez et al (2014) A cytosolic protein factor from the naked mole-rat activates proteasomes of other species and protects these from inhibition. Biochim Biophys Acta 1842 2060 PMID: 25018089
Traister et al (2013) Mutation in integrin-linked kinase (ILK(R211A)) and heat-shock protein 70 comprise a broadly cardioprotective complex. PLoS One 8 e77331 PMID: 24260102
Marada et al (2013) The unfolded protein response selectively targets active smoothened mutants. Mol Cell Biol 33 2375 PMID: 23572559
Wiech et al (2012) Molecular mechanism of mutant p53 stabilization: the role of HSP70 and MDM2. PLoS One 7 e51426 PMID: 23251530
Shorter (2011) The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS One 6 e26319 PMID: 22022600
Boroughs et al (2011) A unique role for heat shock protein 70 and its binding partner tissue transglutaminase in cancer cell migration. J Biol Chem 286 37094 PMID: 21896482
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