Passa al contenuto
Merck
Tutte le immagini(2)

Documenti fondamentali

SAB4200729

Sigma-Aldrich

Anti-Vinculin Antibody

mouse monoclonal, VIN-11-5

Sinonimo/i:

Anti-MV, Anti-Metavinculin, Anti-VINC1

Autenticatiper visualizzare i prezzi riservati alla tua organizzazione & contrattuali


About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

Nome del prodotto

Anti-Vinculin antibody, Mouse monoclonal, clone VIN-11-5, purified from hybridoma cell culture

Origine biologica

mouse

Livello qualitativo

Forma dell’anticorpo

purified from hybridoma cell culture

Tipo di anticorpo

primary antibodies

Clone

VIN-11-5, monoclonal

Stato

buffered aqueous solution

PM

~120 kDa

Reattività contro le specie

human, monkey, rat, mouse, guinea pig, bovine, hamster, chicken, dog

Concentrazione

~1.0 mg/mL

tecniche

immunoblotting: 0.125-0.25 μg/mL using mouse myoblast C2C12 cell extract
immunofluorescence: 5-10 μg/mL
immunohistochemistry: suitable
immunoprecipitation (IP): suitable

Isotipo

IgG1

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

mouse ... Vcl(22330)

Descrizione generale

Anti-Vinculin antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the VIN-11-5 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from a mouse immunized with smooth muscle vinculin from chicken gizzard. Vinculin, also known as metavinculin is highly conserved scaffolding protein localized to focal adhesions and adherens junctions. Vinculin is a 116 kDa protein with 1066 aminoacids. Vinculin comprises eight anti-parallel α-helical bundles organized into five distinct domains. Domains 1-3 are arranged into a tri-lobar head with a molecular mass of 95 kDa and diameter of 80Å . The vinculin head binds many proteins including talin, IpaA, β-catenin, α-catenin and α-actinin. A 61 amino acid, proline-rich linker region (residues 837-878) connects the head and tail. The linker binds vasodilator-stimulated phosphoprotein (VASP), vinexin, ponsin and Arp2/3. The vinculin tail (amino acids 879-1066) is a 30 kDa helical bundle containing five helices connected by short loops (3-8 residues). The tail contains binding sites for vinculin head domain, paxillin, acidic phospholipids and actin. Within the cell vinculin exists either as open, active form or as a closed, auto-inhibited state. The vinculin gene is mapped to human chromosome 10q22.2. Metavinculin (150 kDa), a splice variant of vinculin, is co-expressed with vinculin in muscle tissues. These proteins are localized to the cell membrane, the I-band in the sarcomere and to the intercalated discs.

Immunogeno

smooth muscle vinculin from chicken gizzard

Applicazioni

Monoclonal Anti-Vinculin is recommended to use in various immunochemical assays, including immunoblot (~120kDa), immunofluorescence, immunohistochemistry and immunoprecipitation.

Azioni biochim/fisiol

Vinculin is a cytoplasmic actin binding protein. It plays a key role in cell to cell and cell to matrix adhesion. It mediates adhesion by directly binding to F-actin and subsequently causing actin polymerization and binding of actin remodelling proteins. At high concentrations, Vinculin can undergo oligomerization and may be involved in the transmembrane assembly of adhesion plaques. Vinculin has been implicated in the control of adhesion, cell morphology and motility and muscle functions. Mutations in vinculin, affects the binding of vinculin to F-actin and impairs cell migration. It is a susceptible gene for dilated and hypertrophic cardiomyopathy. Mutations in vinculin may lead to sudden unexplained nocturnal death syndrome (SUNDS). In relation to cell adhesion and motility function, Vinculin is considered to have a crucial effect on tumor cells ability to invade tissues and hence to metastasize. Thus, it is suggested to be implicated in diagnosis of cancer progression and metastasis prognosis.

Stato fisico

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Esclusione di responsabilità

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.

Non trovi il prodotto giusto?  

Prova il nostro Motore di ricerca dei prodotti.

Raccomandato

N° Catalogo
Descrizione
Determinazione del prezzo

Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Scegli una delle versioni più recenti:

Certificati d'analisi (COA)

Lot/Batch Number

Non trovi la versione di tuo interesse?

Se hai bisogno di una versione specifica, puoi cercare il certificato tramite il numero di lotto.

Possiedi già questo prodotto?

I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.

Visita l’Archivio dei documenti

J Thomas Parsons et al.
Nature reviews. Molecular cell biology, 11(9), 633-643 (2010-08-24)
Cell migration affects all morphogenetic processes and contributes to numerous diseases, including cancer and cardiovascular disease. For most cells in most environments, movement begins with protrusion of the cell membrane followed by the formation of new adhesions at the cell
Vinculin in cell-cell and cell-matrix adhesions
Bays JL and DeMali KA
Cellular and Molecular Life Sciences, 74(16), 2999-3009 (2017)
B Geiger et al.
Journal of cell science. Supplement, 8, 251-272 (1987-01-01)
Adherens junctions are members of a molecularly and structurally heterogeneous family of cell contacts sharing a common association with the microfilament system. Various topics related to the biogenesis of these cellular contacts and the molecular interactions involved in their formation
A M Sydor et al.
The Journal of cell biology, 134(5), 1197-1207 (1996-09-01)
Filopodial motility is critical for many biological processes, particularly for axon guidance. This motility is based on altering the F-actin-based cytoskeleton, but the mechanisms of how this occurs and the actin-associated proteins that function in this process remain unclear. We
Porcine vinculin and metavinculin differ by a 68-residue insert located close to the carboxy-terminal part of the molecule.
Gimona M, et al.
The Embo Journal, 7(8), 2329-2334 (1988)

Il team dei nostri ricercatori vanta grande esperienza in tutte le aree della ricerca quali Life Science, scienza dei materiali, sintesi chimica, cromatografia, discipline analitiche, ecc..

Contatta l'Assistenza Tecnica.