S4826
SMIFH2
≥98% (HPLC), actin assembly inhibitor, powder
Synonym(s):
1-(3-Bromophenyl)-5-(2-furanylmethylene)dihydro-2-thioxo-4,6(1H,5H)-pyrimidinedione
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About This Item
Empirical Formula (Hill Notation):
C15H9BrN2O3S
CAS Number:
Molecular Weight:
377.21
UNSPSC Code:
12352200
NACRES:
NA.77
Product Name
SMIFH2, ≥98% (HPLC)
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.
SMIFH2 is an inhibitor of formin-mediated actin assembly that disrupts formin dependent processes.
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Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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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
Anushree C Gulvady et al.
Molecular biology of the cell, 30(11), 1298-1313 (2019-03-21)
Fibroblasts transformed by the proto-oncogene Src form individual invadopodia that can spontaneously self-organize into large matrix-degrading superstructures called rosettes. However, the mechanisms by which the invadopodia can spatiotemporally reorganize their architecture is not well understood. Here, we show that Hic-5
N O Alieva et al.
Nature communications, 10(1), 3593-3593 (2019-08-11)
Filopodia, dynamic membrane protrusions driven by polymerization of an actin filament core, can adhere to the extracellular matrix and experience both external and cell-generated pulling forces. The role of such forces in filopodia adhesion is however insufficiently understood. Here, we