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Key Documents

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SML0271

Sigma-Aldrich

VER-155008

≥98% (HPLC)

Sinónimos:

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

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About This Item

Fórmula empírica (notación de Hill):
C25H23Cl2N7O4
Número de CAS:
1134156-31-2
Peso molecular:
556.40
MDL number:
MFCD18086892
UNSPSC Code:
12352200
PubChem Substance ID:
329825279
NACRES:
NA.77

Quality Level

100

assay

≥98% (HPLC)

form

powder

storage condition

desiccated

color

white to light brown

solubility

DMSO: >10 mg/mL

storage temp.

2-8°C

SMILES string

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

InChI key

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

Biochem/physiol Actions

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).

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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
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
Fang Hu et al.
Cell reports, 26(1), 168-181 (2019-01-04)
The heat shock protein 70 (Hsp70) is upregulated in response to stress and has been implicated as a stress marker in temporal lobe epilepsy (TLE). However, whether Hsp70 plays a pathologic or protective role in TLE remains unclear. Here we
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