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ChemicalBook--->CAS DataBase List--->304684-77-3

304684-77-3

304684-77-3 Structure

304684-77-3 Structure
IdentificationBack Directory
[Name]

2-Methoxy-4-[(5,6,7,8-tetrahydro-benzo[4,5]thieno[2,3-d]pyrimidin-4-yl)-hydrazonomethyl]-phenol
[CAS]

304684-77-3
[Synonyms]

Exo2
Exo2 >=98% (HPLC)
2-Methoxy-4-[(5,6,7,8-tetrahydro-benzo[4,5]thieno[2,3-d]pyrimidin-4-yl)-hydrazonomethyl]-phenol
[Molecular Formula]

C18H18N4O2S
[MDL Number]

MFCD00380179
[MOL File]

304684-77-3.mol
[Molecular Weight]

354.43
Chemical PropertiesBack Directory
[Boiling point ]

591.0±50.0 °C(Predicted)
[density ]

1.44±0.1 g/cm3(Predicted)
[storage temp. ]

2-8°C
[solubility ]

DMSO: >20mg/mL
[form ]

powder
[pka]

8.79±0.35(Predicted)
[color ]

yellow
[Stability:]

Stable for 1 year from date of purchase as supplied. Solutions in DMSO may be stored at -20°C for up to 1 month.
Safety DataBack Directory
[WGK Germany ]

3
Hazard InformationBack Directory
[Description]

Exo2 (304684-77-3) disrupts the Golgi apparatus and stimulates Golgi-ER fusion in mammalian cells.1 May be used to completely ablate the Golgi apparatus.1 Like brefeldin A (BFA), it inhibits anterograde transport and disrupts morphology of the trans-Golgi network (TGN) but unlike BFA, it does not induce tubulation and merging of the TGN and endosomal compartments.2? It perturbs trafficking of Shiga toxin between endosomes and the trans-Golgi network, in contrast to cholera toxin.1,2 Accelerates degradation of perilipin-2 proteins.3
[Definition]

ChEBI: Exo2 is a member of phenols and a member of methoxybenzenes.
[References]

1) Feng et al. (2004), Retrograde transport of cholera toxin from the plasma membrane to the endoplasmic reticulum requires the trans-Golgi network but not the Golgi apparatus in Exo2-treated cells; EMBO Rep., 5 596 2) Spooner et al. (2008), The secretion inhibitor Exo2 perturbs trafficking of Shiga toxin between endosomes and the trans-Golgi network; Biochem. J., 414 471 3) Pauloin et al. (2016), The perilipin-2 (adipophilin) coat of cytosolic lipid droplets is regulated by an Arf1-dependent mechanism in the HC11 mouse mammary epithelial cells; Cell Biol. Int., 40 143
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