Anti-Vinculin Antibody

Anti-Vinculin antibody produced in rabbit has been used in immunoprecipitation.

Anti-vinculin antibody produced in rabbit has been used in following studies:

• immunofluorescence
• immuno-histology
• western blotting

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.

Vinculin also binds α-catenin as well as the vasodilator stimulated phosphoprotein (VASP) in focal contact assembly. It transiently binds the actin-related protein-2/3 (ARP2/3) complex without colocalization in focal adhesions.

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In muscle, vinculin is localized in the fascia adherens of the intercalated disk (cardiac muscle), myotendinous junctions (skeletalmuscle), neuromuscular junctions, and the membrane associated dense bodies of smooth muscle. In many cell types undergoing viral transformation, vinculin becomes redistributed to rosettes or podosomes.

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.

synthetic peptide corresponding to amino acid residues 691-705 of human vinculin with N-terminal added cysteine, conjugated to KLH. This sequence is also present in metavinculin. The corresponding sequence is identical is mouse, rat, and pig and differs by one amino acid in chicken.

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