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V9264

Sigma-Aldrich

Anti-Vinculin 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:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

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

packaging

antibody small pack of 25 μL

concentration

~1.0 mg/mL

technique(s)

immunocytochemistry: 5-10 μg/mL using HS-68 human fibroblast cell culture
immunohistochemistry: suitable
indirect ELISA: suitable
western blot: 0.05-0.1 μg/mL using HS-68 total cell extract

isotype

IgG1

UniProt accession no.

application(s)

research pathology

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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General description

Anti-Vinculin antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the hVIN-1 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with vinculin purified from human uterus. Vinculin is a cytoskeletal protein associated with the cytoplasmic faces of both cell-cell and cell-extracellular matrix adherens-type junctions. In muscle, vinculin is localized in the fascia adherens of the intercalated disk (cardiac muscle), myotendinous junctions (skeletal muscle), neuromuscular junctions, and the membrane associated dense bodies of smooth muscle.

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

Anti-Vinculin antibody, Mouse monoclonal has been used in
  • immunoblotting
  • immunofluorescence staining
  • immunocytochemistry
  • immunohistochemistry and enzyme linked immunosorbent assay (ELISA).

Biochem/physiol Actions

Vinculin functions as one of several interacting proteins involved in anchoring F-actin to the membrane. It has been shown that a sequence of molecular interactions might be involved in the transmembrane assembly of adhesion plaques. vinculin represents a key element in the transmembrane linkage of the extracellular matrix to the cytoplasmic microfilament system. In many cell types undergoing viral transformation, vinculin becomes redistributed to rosettes or podosomes.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 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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Storage Class

12 - Non Combustible Liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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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Highly conserved testicular localization of claudin-11 in normal and impaired spermatogenesis
Stammler A, et al.
Testing, 11(8), e0160349-e0160349 (2016)
Podosomes as smart regulators of cellular adhesion
Spinardi L and Marchisio PC
European Journal of Cell Biology, 85(3-4), 191-194 (2006)
Functional importance of Dicer protein in the adaptive cellular response to hypoxia
Ho JJD, et al.
Test, 287(34), 29003-29020 (2012)
Enhancing integrin alpha1 inserted (I) domain affinity to ligand potentiates integrin alpha1beta1-mediated down-regulation of collagen synthesis
Shi M, et al.
The Journal of Biological Chemistry, 287(42), 35139-35152 (2012)
Shiqiong Hu et al.
Molecular biology of the cell, 22(17), 3120-3126 (2011-07-09)
Podosomes are dynamic, actin-containing adhesion structures that collectively self-organize as rings. In this study, we first show by observing osteoclasts plated on bead-seeded soft substrates that podosome assemblies, such as rings, are involved in tension forces. During the expansion of

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