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344092

Sigma-Aldrich

Formin FH2 Domain Inhibitor, SMIFH2

The Formin FH2 Domain Inhibitor, SMIFH2, also referenced under CAS 340316-62-3, controls the biological activity of Formin FH2 Domain. This small molecule/inhibitor is primarily used for Membrane applications.

Synonyme(s) :

Formin FH2 Domain Inhibitor, SMIFH2, Small Molecule Inhibitor of Formin Homology 2 domain, 1-(3-Bromophenyl)-5-(2-furylmethylene)-2-thioxo-hexahydropyrimidine-4,6-dione, Actin Assembly Inhibitor XV

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About This Item

Formule empirique (notation de Hill):
C15H9BrN2O3S
Numéro CAS:
Poids moléculaire :
377.21
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.28

Niveau de qualité

Pureté

≥98% (sum of two geometrical isomers, HPLC)

Forme

solid

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

OK to freeze
protect from light

Couleur

darkdeep green

Solubilité

DMSO: 50 mg/mL

Conditions d'expédition

ambient

Température de stockage

2-8°C

InChI

1S/C15H9BrN2O3S/c16-9-3-1-4-10(7-9)18-14(20)12(13(19)17-15(18)22)8-11-5-2-6-21-11/h1-8H,(H,17,19,22)/b12-8+

Clé InChI

MVFJHEQDISFYIS-XYOKQWHBSA-N

Description générale

A cell-permeable thiooxodihydropyrimidinedione compound that inhibits both formin-mediated, profilin-independent actin nucleation (IC50 ~15 µM using mDia1 or mDia2) and formin-mediated elongation of actin filaments in the presence of profilin (IC50 ~4 µM using Cdc12 or mDia2), but not the Arp2/3-mediated or formin-independent actin assembly. SMIFH2 targets the FH2 (formin homology 2) domain of formins from a large variety of species, including murine mDia1/2, C. elegans CYK-1, S. pombe Cdc12, S. pombe Fus1, and S. cerevisiae Bni1, and decreases formin affinity for the actin filament barbed end. SMIFH2, at 25 µM, is shown to selectively disrupt formin-dependent actin cables and contractile rings, but not Arp2/3-dependent, CK-666- (Cat. No. 182515) sensitive actin patches, in fission yeast. SMIFH2 is also demonstrated to affect F-actin cytoskeleton structures and cell migration (by a 2-fold decrease at 10 µM) in NIH 3T3 fibroblast cultures.
A cell-permeable thiooxodihydropyrimidinedione compound that inhibits both formin-mediated, profilin-independent actin nucleation (IC50 ~15 µM using mDia1 or mDia2) and formin-mediated elongation of actin filaments in the presence of profilin (IC50 ~4 µM using Cdc12 or mDia2), but not the Arp2/3-mediated or formin-independent actin assembly. SMIFH2 targets the FH2 (formin homology 2) domain of formins from a large variety of species, including murine mDia1/2, C. elegans CYK-1, S. pombe Cdc12, S. pombe Fus1, and S. cerevisiae Bni1, and decreases formin affinity for the actin filament barbed end. SMIFH2, at 25 µM, is shown to selectively disrupt formin-dependent actin cables and contractile rings, but not Arp2/3-dependent, CK-666- (Cat. No. 182515) sensitive actin patches, in fission yeast. SMIFH2 is also demonstrated to affect F-actin cytoskeleton structures and cell migration (by a 2-fold decrease at 10 µM) in NIH 3T3 fibroblast cultures.

Conditionnement

Packaged under inert gas

Avertissement

Toxicity: Standard Handling (A)

Reconstitution

Use only fresh DMSO. Following reconstiution, aliquot an freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.

Autres remarques

Rizvi, S.A., et al. 2009. Chem. Biol.16, 1158.

Informations légales

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

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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Shintaro Miyazaki et al.
iScience, 26(5), 106594-106594 (2023-05-30)
It has been reported that the MDCK cell tight junction shows stochastic fluctuation and forms the interdigitation structure, but the mechanism of the pattern formation remains to be elucidated. In the present study, we first quantified the shape of the
Tushna Kapoor et al.
Cell reports, 34(13), 108918-108918 (2021-04-01)
Membrane curvature recruits Bin-Amphiphysin-Rvs (BAR)-domain proteins and induces local F-actin assembly, which further modifies the membrane curvature and dynamics. The downstream molecular pathway in vivo is still unclear. Here, we show that a tubular endomembrane scaffold supported by contractile actomyosin stabilizes
Jia C Wang et al.
eLife, 11 (2022-04-12)
B-cell activation and immune synapse (IS) formation with membrane-bound antigens are actin-dependent processes that scale positively with the strength of antigen-induced signals. Importantly, ligating the B-cell integrin, LFA-1, with ICAM-1 promotes IS formation when antigen is limiting. Whether the actin
Daniel Blumenthal et al.
eLife, 9 (2020-07-29)
T cell activation by dendritic cells (DCs) involves forces exerted by the T cell actin cytoskeleton, which are opposed by the cortical cytoskeleton of the interacting antigen-presenting cell. During an immune response, DCs undergo a maturation process that optimizes their
Syncytin-mediated open-ended membrane tubular connections facilitate the intercellular transfer of cargos including Cas9 protein.
Zhang, et al.
eLife, 12 (2023)

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