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SAB4200147

Sigma-Aldrich

Anti-FHOD1 antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

Synonyma:

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

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen


About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

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)

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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Storage Class

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


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Navštívit knihovnu dokumentů

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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