Cell Signaling Technology

Product Pathways - Adhesion

Vinculin Antibody #4650

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Mk Dg Endogenous 124 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  Dg=Dog
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

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

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.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell and tissue types using Vinculin Antibody.

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 confirmation. 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 recently demonstrated relationship between decreased vinculin expression and increased carcinogenesis and metastasis in colorectal carcinoma (9).

  1. Izard, T. et al. (2004) Nature 427, 171-5.
  2. Humphries, J.D. et al. (2007) J Cell Biol 179, 1043-57.
  3. Witt, S. et al. (2004) J Biol Chem 279, 31533-43.
  4. Xu, W. et al. (1998) Development 125, 327-37.
  5. Ziegler, W.H. et al. (2002) J Biol Chem 277, 7396-404.
  6. Zhang, Z. et al. (2004) Mol Biol Cell 15, 4234-47.
  7. Rodríguez Fernández, J.L. et al. (1993) J Cell Biol 122, 1285-94.
  8. Samuels, M. et al. (1993) J Cell Biol 121, 909-21.
  9. Yang, H.J. et al. (2010) Cancer Invest 28, 127-34.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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