S4826
SMIFH2
≥98% (HPLC), actin assembly inhibitor, powder
동의어(들):
1-(3-Bromophenyl)-5-(2-furanylmethylene)dihydro-2-thioxo-4,6(1H,5H)-pyrimidinedione
제품 이름
SMIFH2, ≥98% (HPLC)
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
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
Quality Level
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.
SMIFH2 is an inhibitor of formin-mediated actin assembly that disrupts formin dependent processes.
저장 등급
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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
Sarah J Copeland et al.
Molecular biology of the cell, 29(13), 1611-1627 (2018-05-10)
A primary cilium is found on most mammalian cells, where it acts as a cellular antenna for the reception of both mechanical and chemical signals. A variety of diseases are associated with defective ciliogenesis, reflecting the ubiquity of the function
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