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F7053

Sigma-Aldrich

Anti-Vinculin−FITC antibody, Mouse monoclonal

clone hVIN-1, purified from hybridoma cell culture

Synonym(s):

Monoclonal Anti-Vinculin antibody produced in mouse

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About This Item

MDL number:
MFCD00162905
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

FITC conjugate

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

hVIN-1, monoclonal

form

buffered aqueous solution

mol wt

antigen 116 kDa

species reactivity

frog, chicken, mouse, canine, human, bovine, rat, turkey

storage condition

protect from light

technique(s)

direct immunofluorescence: 1:50 using methanol/acetone fixed cultured bovine MDBK cells

isotype

IgG1

UniProt accession no.

P18206

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... VCL(7414)
mouse ... Vcl(22330)
rat ... Vcl(305679)

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Specificity

Specifically labels vinculin at cell-cell and cell-substrate contacts. Reacts strongly with human vinculin. Shows cross-reactivity with smooth muscle metavinculin.

Immunogen

purified human vinculin from uterus.

Application

Monoclonal Anti-Vinculin-FITC antibody is suitable for immunofluorescence staining of fibroblasts cells to study the effects of nanofiber spatial organization on cell behaviors. It is also suitable for direct immunofluorescence at a dilution of 1:50 using methanol/acetone fixed cultured bovine MDBK cells.

Biochem/physiol Actions

Vinculin is a cytoskeletal protein with molecular mass of ~116 kDa. Vinculin is closely associated with adhesive membrane areas, such as focal contacts, podosomes, or intercellular junctions of the zonula adherens type. It acts as a mediator in interactions of integrins and the actin cytoskeleton. It forms a bridge between integrins, receptors for ECM molecules on the cell surface and the F-actin cytoskeleton. It is associated with talin and α-actinin which directly connects with integrins. It has ability to bind α-catenin as well as the vasodilator stimulated phosphoprotein (VASP) in focal contact assembly.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

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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Description
Pricing

Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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E E Weiss et al.
The Journal of cell biology, 141(3), 755-764 (1998-06-13)
In epithelial cells, alpha-, beta-, and gamma-catenin are involved in linking the peripheral microfilament belt to the transmembrane protein E-cadherin. alpha-Catenin exhibits sequence homologies over three regions to vinculin, another adherens junction protein. While vinculin is found in cell-matrix and
Leonel E Rojo et al.
Journal of cosmetic dermatology, 9(3), 185-195 (2010-10-05)
Cell migration, angiogenesis, inflammation, and extracellular matrix remodeling are key events in wound healing. Natural products, including fatty acids (FAs), can accelerate wound healing by modulating the aforementioned events. This study aims to evaluate the effect of lucuma (Pouteria lucuma
Carol Jurchenko et al.
Biophysical journal, 106(7), 1436-1446 (2014-04-08)
The interplay between chemical and mechanical signals plays an important role in cell biology, and integrin receptors are the primary molecules involved in sensing and transducing external mechanical cues. We used integrin-specific probes in molecular tension fluorescence microscopy to investigate
A Westmeyer et al.
The EMBO journal, 9(7), 2071-2078 (1990-07-01)
We have analyzed the functional domain structure of vinculin, a protein involved in linking microfilaments to the cytoplasmic face of cell membranes in animal cells. For this purpose, we used several monoclonal antibodies raised against chicken gizzard vinculin whose epitopes
Mathieu Maalouf et al.
Nanomaterials (Basel, Switzerland), 12(10) (2022-05-29)
Ultrashort pulse lasers have significant advantages over conventional continuous wave and long pulse lasers for the texturing of metallic surfaces, especially for nanoscale surface structure patterning. Furthermore, ultrafast laser beam polarization allows for the precise control of the spatial alignment
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