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Merck
CN

V4889

Anti-phospho-Vinculin (pTyr822) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-CMD1W, Anti-CMH15, Anti-HEL114, Anti-MV, Anti-MVCL

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41
MDL number:
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Product Name

Anti-phospho-Vinculin (pTyr822) antibody produced in rabbit, affinity isolated antibody, buffered aqueous solution

Quality Level

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human, chicken, rat, mouse

technique(s)

western blot: 1:1,000 using chick embryo fibroblasts (CEFs) transfected with activated Src.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

phosphorylation (pTyr822)

Gene Information

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

Related Categories

Application

Anti-phospho-Vinculin (pTyr822) antibody produced in rabbit has been used in immunofluorescence staining.

Biochem/physiol Actions

Vinculin (VCL) is a cytoskeletal protein that supports cell-to-cell and cell to matrix junctions. It is also essentially involved in normal embryonic development and cardiac function, due to its role in controlling adhesion and motility, as well as cell spreading.In mature focal adhesions (FAs), VCL acts as an important constituent of the “molecular clutch” that induces the transmission of force from cytoplasmic F-actin to membrane-bound integrins. Aberration or mutation of VCL leads to cardiomyopathy, which is associated with hypertension. Experimental studies reveal that, VCL might be used as a biomarker of aging or heart failure. Vinculin associates with FAs and assists in several cellular functions, such as stabilizing and strengthening FAs and promoting their maturation, extracellular matrix (ECM) mechanosensing, regulating actin cytoskeletal dynamics and signaling pathways involved in apoptosis.

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.

General description

Vinculin (VCL) is a ubiquitously expressed cytoskeletal protein, encoded by the gene mapped to human chromosome 10q11.2-qter. VCL is a vital element of adherens type cell junctions. Vinculin structure contains a globular head connected to a tail domain by a short proline-rich sequence, and an intramolecular interaction between the head and tail hides the various ligand-binding sites in the protein.

Immunogen

synthetic phosphopeptide derived from the region of vinculin that contains tyrosine 822.

Physical form

Solution in Dulbecco′s phosphate buffered saline (without Mg2+ and Ca2+), pH 7.3, with 50% glycerol, 1.0 mg/mL BSA (IgG and protease free) and 0.05% sodium azide.

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Storage Class

10 - Combustible liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

Regulatory Information

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Molecular mechanism of transglutaminase-2 in corneal epithelial migration and adhesion
Tong L
Biochimica et Biophysica Acta, 1833, 1304-1315 (2013)
Sex-specific association of rs4746172 of VCL gene with hypertension in two Han populations from Southern China.
Yu Q
Scientific Reports (2015)
The structure and regulation of vinculin.
Ziegler WH
Trends in Cell Biology, 16, 453-460 (2006)
Complementary physical and genetic techniques map the vinculin (VCL) gene on chromosome 10q.
Mulligan LM
Genomics, 13, 1347-1349 (1992)
Tina Izard et al.
The Journal of biological chemistry, 291(6), 2548-2555 (2016-01-06)
The cytoskeletal protein vinculin is a major regulator of cell adhesion and attaches to the cell surface by binding to specific phospholipids. Structural, biochemical, and biological studies provided much insight into how vinculin binds to membranes, what components it recognizes

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