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SML2332

Sigma-Aldrich

Dynarrestin

≥98% (HPLC)

Synonyme(s) :

4-(4-Diethylaminophenyl)-2-(2,4-difluoro-phenylamino)-thiazole-5-carboxylic acid ethyl ester

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About This Item

Formule empirique (notation de Hill):
C22H23F2N3O2S
Numéro CAS:
2222768-84-3
Poids moléculaire :
431.50
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.77

Pureté

≥98% (HPLC)

Forme

powder

Couleur

white to brown

Solubilité

DMSO: 2 mg/mL, clear

Température de stockage

2-8°C

Chaîne SMILES 

CCN(CC)C1=CC=C(C2=C(C(OCC)=O)SC(NC3=C(F)C=C(F)C=C3)=N2)C=C1

Actions biochimiques/physiologiques

Dynarrestin is a potent and selective reversible inhibitor of cytoplasmic dyneins 1 and 2 that inhibits dynein 1-dependent microtubule binding and motility without affecting ATP hydrolysis. It inhibits endosome movement and disturbs mitosis in cells. Dynarrestin inhibits dynein 2-mediated intraflagellar transport of the cargo IFT88 and flux of Smo within cilia. Also it inhibits cancer cells proliferation downstream of Smo.
Dynarrestin is an aminothiazole derivative, which can bind to protein tyrosine phosphatase interacting protein 51 (PTPIP51). This interaction helps in regulating various signaling pathways that lead to proliferation and migration. Dynarrestin blocks hedgehog (Hh)-dependent signaling in mouse and human cells.

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

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Eric Dietel et al.
PloS one, 14(5), e0216642-e0216642 (2019-05-11)
LDC3/Dynarrestin, an aminothiazole derivative, is a recently developed small molecule, which binds protein tyrosine phosphatase interacting protein 51 (PTPIP51). PTPIP51 interacts with various proteins regulating different signaling pathways leading to proliferation and migration. Her2 positive breast cancer cells (SKBR3) express
Nicholas M Zehrbach et al.
Molecular biology of the cell, 34(7), ar65-ar65 (2023-04-13)
Rab GTPase-mediated vesicle trafficking of cell surface proteins, including integrins, through endocytic and recycling pathways is important in controlling cell-extracellular matrix interactions during cell migration. The focal adhesion adaptor protein, paxillin, plays a central role in regulating adhesion dynamics and
Ariane Schleinitz et al.
Cell reports, 42(1), 111969-111969 (2023-01-15)
The transfer of endocytosed cargoes to lysosomes (LYSs) requires HOPS, a multiprotein complex that tethers late endosomes (LEs) to LYSs before fusion. Many proteins interact with HOPS on LEs/LYSs. However, it is not clear whether these HOPS interactors localize to
Susanne Höing et al.
Cell chemical biology, 25(4), 357-369 (2018-02-06)
Aberrant hedgehog (Hh) signaling contributes to the pathogenesis of multiple cancers. Available inhibitors target Smoothened (Smo), which can acquire mutations causing drug resistance. Thus, compounds that inhibit Hh signaling downstream of Smo are urgently needed. We identified dynarrestin, a novel
Yunan Ye et al.
EMBO reports, 23(11), e55251-e55251 (2022-10-11)
Microtubules typically promote nuclear centring during early embryonic divisions in centrosome-containing vertebrates. In acentrosomal mouse zygotes, microtubules also centre male and female pronuclei prior to the first mitosis, this time in concert with actin. How nuclear centring is brought about

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