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Key Documents

SML0271

Sigma-Aldrich

VER-155008

≥98% (HPLC)

Synonyme(s) :

5′-O-[(4-Cyanophenyl)methyl]-8-[[(3,4-dichlorophenyl)methyl]amino]-adenosine

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About This Item

Formule empirique (notation de Hill):
C25H23Cl2N7O4
Numéro CAS:
Poids moléculaire :
556.40
Numéro MDL:
Code UNSPSC :
12352200
ID de substance PubChem :
Nomenclature NACRES :
NA.77

Niveau de qualité

Pureté

≥98% (HPLC)

Forme

powder

Conditions de stockage

desiccated

Couleur

white to light brown

Solubilité

DMSO: >10 mg/mL

Température de stockage

2-8°C

Chaîne SMILES 

Nc1ncnc2n([C@@H]3O[C@H](COCc4ccc(cc4)C#N)[C@@H](O)[C@H]3O)c(NCc5ccc(Cl)c(Cl)c5)nc12

InChI

1S/C25H23Cl2N7O4/c26-16-6-5-15(7-17(16)27)9-30-25-33-19-22(29)31-12-32-23(19)34(25)24-21(36)20(35)18(38-24)11-37-10-14-3-1-13(8-28)2-4-14/h1-7,12,18,20-21,24,35-36H,9-11H2,(H,30,33)(H2,29,31,32)/t18-,20-,21-,24-/m1/s1

Clé InChI

ZXGGCBQORXDVTE-UMCMBGNQSA-N

Application

VER-155008 has been used as a heat shock protein 70 (HSP70) inhibitor:
  • to study its effects on human embryonic kidney 293 (HEK293T) cells
  • to study its effects on viral mRNA synthesis and protein expression in Vero E6 cells
  • to determine its effects on the attenuation of seizures in rats

Actions biochimiques/physiologiques

VER-155002 is a small molecule, ATP-derivative inhibitor of HSP70 (IC50 = 500 nM). The compound inhibits proliferation of several colon and breast cancer cell lines, induces caspase dependent apoptosis in BT474 cells and down regulates expression of Her2 and Raf-1 in HCT116 cells.
VER‐155008 positively promotes memory recovery and axonal regrowth. It is also involved in inhibiting cell cycle progression and proliferation in non-small-cell lung cancer (NSCLC).

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Wen-Jing Zhang et al.
Virology, 553, 70-80 (2020-11-27)
Many viruses utilize molecular chaperone heat shock protein 90 (Hsp90) for protein folding and stabilization, however, the role of Hsp90 in herpesvirus lifecycle is obscure. Here, we provide evidence that Hsp90 participates in pseudorabies virus (PRV) replication. Viral growth kinetics
Wei Wen et al.
Experimental biology and medicine (Maywood, N.J.), 239(5), 638-645 (2014-03-29)
Lung cancer is the most common malignancy and exhibits significant morbidity and mortality worldwide. Among all lung cancer subtypes, non-small-cell lung cancer (NSCLC) accounts for the majority of all lung cancer cases. Although there have been intensive investigations on the
Eunmi Lee et al.
Oncogene, 38(4), 469-482 (2018-09-01)
TNFα is a pleiotropic cytokine which fuels tumor cell growth, invasion, and metastasis in some malignancies, while in others it induces cytotoxic cell death. However, the molecular mechanism by which TNFα exerts its diverse effects on breast cancer subtypes remains
Ximeng Yang et al.
Frontiers in pharmacology, 9, 48-48 (2018-02-15)
Alzheimer's disease (AD) is a progressive neurodegenerative disorder resulting in structural brain changes and memory impairment. We hypothesized that reconstructing neural networks is essential for memory recovery in AD. Heat shock cognate 70 (HSC70), a member of the heat shock
Miriam Schäfer et al.
FEBS letters, 591(21), 3567-3587 (2017-09-28)
The shedding of ectodomains is a crucial mechanism in many physiological and pathological events. A disintegrin and metalloprotease-17 (ADAM17) is a key sheddase involved in essential processes, such as development, regeneration, and immune defense. ADAM17 exists in two conformations which

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