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Merck
CN

SAB4200147

Sigma-Aldrich

Anti-FHOD1 antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

别名:

Anti-FH1/FH2 domain-containing protein 1, Anti-FHOS, Anti-Formin homology-2 domain-containing protein 1, Anti-formin homolog overexpressed in spleen 1, Anti-formin homology 2 domain-containing protein 1

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About This Item

UNSPSC代码:
12352203
NACRES:
NA.41

生物来源

rabbit

质量水平

偶联物

unconjugated

抗体形式

affinity isolated antibody

抗体产品类型

primary antibodies

克隆

polyclonal

形式

buffered aqueous solution

分子量

~130 kDa

种属反应性

human

包装

antibody small pack of 25 μL

浓度

~1.0 mg/mL

技术

immunohistochemistry: 10-20 μg/mL using heat-retrieved formalin-fixed, paraffin-embedded human spleen sections and biotin, ExtrAvidin® peroxidase staining system
western blot: 0.5-1.0 μg/mL using whole extracts of human K562 cells

UniProt登记号

运输

dry ice

储存温度

−20°C

靶向翻译后修饰

unmodified

基因信息

human ... FHOD1(29109)

一般描述

Formin homology domain protein 1 (FHOD1) is an important endothelial formin. It is also called as Fhos1. FHOD1 is located on human chromosome 16q22.

应用

Anti-FHOD1 antibody has been used in western blotting.

生化/生理作用

Formin homology domain protein 1 (FHOD1) participates in actin reorganization in vascular endothelial cells, stimulated by thrombin. It plays an important role in the generation of stress fibres in vascular endothelial cells. FHOD1 is considered as a therapeutic target to modulate endothelial permeability.

法律信息

ExtrAvidin is a registered trademark of Merck KGaA, Darmstadt, Germany

免责声明

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

常规特殊物品

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The mammalian formin FHOD1 is activated through phosphorylation by ROCK and mediates thrombin-induced stress fibre formation in endothelial cells.
Takeya R, et al.
The Embo Journal, 27(4), 618-628 (2008)
Pascale Monzo et al.
Molecular biology of the cell, 27(8), 1246-1261 (2016-02-26)
Glioblastomas are extremely aggressive brain tumors with highly invasive properties. Brain linear tracks such as blood vessel walls constitute their main invasive routes. Here we analyze rat C6 and patient-derived glioma cell motility in vitro using micropatterned linear tracks to
Mechanical confinement triggers glioma linear migration dependent on formin FHOD3.
Monzo P, et al.
Molecular Biology of the Cell, 27(8), 1246-1261 (2016)
Xuemeng Shi et al.
Journal of molecular cell biology, 13(12), 876-888 (2021-11-01)
Both the mechanosensitive actin cytoskeleton and caveolae contribute to active processes such as cell migration, morphogenesis, and vesicular trafficking. Although distinct actin components are well studied, how they contribute to cytoplasmic caveolae, especially in the context of mechano-stress, has remained
Shuangshuang Zhao et al.
Cytoskeleton (Hoboken, N.J.), 77(1-2), 16-24 (2019-12-11)
Formins and tropomyosins (Tpms) are two central components of the microfilaments. Formins are involved in the nucleation and polymerization of actin filaments, and Tpms form along the actin stress fibers to regulate their dynamics. However, the correlation between formins and

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