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S4826

Sigma-Aldrich

SMIFH2

≥98% (HPLC)

Synonyma:

1-(3-Bromophenyl)-5-(2-furanylmethylene)dihydro-2-thioxo-4,6(1H,5H)-pyrimidinedione

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen


About This Item

Empirický vzorec (Hillův zápis):
C15H9BrN2O3S
Číslo CAS:
Molekulová hmotnost:
377.21
UNSPSC Code:
12352200
NACRES:
NA.77

Quality Level

assay

≥98% (HPLC)

form

powder

storage condition

protect from light

color

light yellow to yellow-green

solubility

DMSO: 20 mg/mL, clear

storage temp.

2-8°C

SMILES string

S=C1N(C(=O)\C(=C\c3[o]ccc3)\C(=O)N1)c2cc(ccc2)Br

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+

InChI key

MVFJHEQDISFYIS-XYOKQWHBSA-N

Application

SMIFH2 was used to decipher the role of mDia2 in controlling microtubule dynamics and myofibroblast differentiation.1

Biochem/physiol Actions

SMIFH2 is an inhibitor of formin homology 2 domains. The compound is a first small molecule inhibitor of formin-mediated actin assembly that disrupts formin dependent processes from yeast to mammals. SMIFH2 may be a useful drug for identifying cellular processes dependent on formin-mediated actin assembly in a broad range of experimental systems. Formin is an actin nucleation factor.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Joseph H R Hetmanski et al.
PLoS computational biology, 17(3), e1008213-e1008213 (2021-03-11)
Cell migration in 3D microenvironments is a complex process which depends on the coordinated activity of leading edge protrusive force and rear retraction in a push-pull mechanism. While the potentiation of protrusions has been widely studied, the precise signalling and
Chang Liu et al.
Molecular plant, 11(11), 1389-1399 (2018-10-09)
The process of pollen germination is crucial for flowering plant reproduction, but the mechanisms through which pollen grains establish polarity and select germination sites are not well understood. In this study, we report that a formin family protein, AtFH5, is localized
Yukako Nishimura et al.
Journal of cell science, 134(8) (2021-02-17)
The small molecular inhibitor of formin FH2 domains, SMIFH2, is widely used in cell biological studies. It inhibits formin-driven actin polymerization in vitro, but not polymerization of pure actin. It is active against several types of formin from different species.
Keith P Eidell et al.
Journal of cell science, 134(16) (2021-07-20)
Integrin engagement within the immune synapse enhances T cell activation, but our understanding of this process is incomplete. In response to T cell receptor (TCR) ligation, SLP-76 (LCP2), ADAP (FYB1) and SKAP55 (SKAP1) are recruited into microclusters and activate integrins
Daan Vorselen et al.
eLife, 10 (2021-10-29)
Phagocytosis requires rapid actin reorganization and spatially controlled force generation to ingest targets ranging from pathogens to apoptotic cells. How actomyosin activity directs membrane extensions to engulf such diverse targets remains unclear. Here, we combine lattice light-sheet microscopy (LLSM) with

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