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Merck
CN

S4826

Sigma-Aldrich

SMIFH2

≥98% (HPLC)

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别名:
1-(3-溴苯基)-5-(2-呋喃基亚甲基)二氢-2-硫代-4,6(1H,5H)-嘧啶二酮
经验公式(希尔记法):
C15H9BrN2O3S
分子量:
377.21
UNSPSC代码:
12352200
NACRES:
NA.77

质量水平

检测方案

≥98% (HPLC)

形式

powder

储存条件

protect from light

颜色

light yellow to yellow-green

溶解性

DMSO: 20 mg/mL, clear

储存温度

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+

InChI key

MVFJHEQDISFYIS-XYOKQWHBSA-N

应用

SMIFH2被用于破译mDia2在控制微管动力学和肌成纤维细胞分化中的作用。1

生化/生理作用

SMIFH2是formin同源2结构域的抑制剂。该化合物是formin介导的肌动蛋白组装的第一种小分子抑制剂,它能够破坏从酵母到哺乳动物的formin依赖性过程。 SMIFH2可作为在各种实验系统中鉴定依赖于formin介导的肌动蛋白组装的细胞过程的有用药物。Formin是一种肌动蛋白成核因子。

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°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
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
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

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