biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
~130 kDa
species reactivity
human
packaging
antibody small pack of 25 μL
concentration
~1.0 mg/mL
technique(s)
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 accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... FHOD1(29109)
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General description
Formin homology domain protein 1 (FHOD1) is an important endothelial formin. It is also called as Fhos1. FHOD1 is located on human chromosome 16q22.
Application
Anti-FHOD1 antibody has been used in western blotting.
Biochem/physiol Actions
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.
Legal Information
ExtrAvidin is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
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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存储类别
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
低风险生物材料
此项目有
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)
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
Mechanical confinement triggers glioma linear migration dependent on formin FHOD3.
Monzo P, et al.
Molecular Biology of the Cell, 27(8), 1246-1261 (2016)
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
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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