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Merck

S4826

SMIFH2

≥98% (HPLC), actin assembly inhibitor, powder

Synonyme(s) :

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

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A propos de cet article

Formule empirique (notation de Hill) :
C15H9BrN2O3S
Numéro CAS:
Poids moléculaire :
377.21
UNSPSC Code:
12352200
NACRES:
NA.77
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Nom du produit

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.

Classe de stockage

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Consulter la Bibliothèque de documents

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
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

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