Render Target: STATIC
Render Timestamp:
5/21/2026, 6:35:31 AM EDT
5/21/2026, 10:35:31 AM UTC
Commit: 7ed46ecc04b401f23a28df741b5078df405d23e4
XML generation date: 2025-11-13 17:58:25.969
Product last modified at: 2026-03-20T08:03:32.608Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Vinculin Antibody #4650

Filter:
  • WB

    Product Specifications

    REACTIVITY H M R Mk Dg
    SENSITIVITY Endogenous
    MW (kDa) 124
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 
    • Dg-Dog 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Simple Western™ 1:10 - 1:50

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Vinculin Antibody detects endogenous levels of total vinculin protein. This antibody also reacts with metavinculin, a 145 kDa splice variant of vinculin.

    Species Reactivity:

    Human, Mouse, Rat, Monkey, Dog

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human vinculin protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Vinculin is a cytoskeletal protein that plays an important role in the regulation of focal adhesions and embryonic development (1-4). Three structural vinculin domains include an amino-terminal head, a short, flexible proline-rich region, and a carboxy-terminal tail (1). In the inactive state, the head and tail domains of vinculin interact to form a closed conformation. The open and active form of vinculin translocates to focal adhesions, where it is thought to be involved in anchoring F-actin to the membrane and regulation of cell migration (2). Phospholipid binding to the tail domain and subsequent phosphorylation of vinculin at Ser1033 and Ser1045 by PKC-α and Tyr100 and Tyr1065 by Src kinases weakens the head-tail interaction (5,6). This change in vinculin allows the binding of a number of other proteins, including talin, α-actinin, and paxillin, which disrupts the head-tail interaction and initiates the conformational change from the inactive to active state (2,4). Vinculin deficiencies are associated with a decrease in cell adhesion and an increase in cell motility, suggesting a possible role in metastatic growth (7,8). This is supported by a demonstrated relationship between decreased vinculin expression and increased carcinogenesis and metastasis in colorectal carcinoma (9).

    Alternate Names

    CMD1W; CMH15; epididymis luminal protein 114; epididymis secretory sperm binding protein; HEL114; meta-vinculin; Metavinculin; MV; MVCL; VCL; VINC; Vinculin; Vinculin iso2

    For Research Use Only. Not for Use in Diagnostic Procedures.
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