Vinculin Antibody #4650
- WB
Supporting Data
| 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™ | 1:50 - 1:250 |
Storage
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 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 demonstrated relationship between decreased vinculin expression and increased carcinogenesis and metastasis in colorectal carcinoma (9).
- Izard, T. et al. (2004) Nature 427, 171-5.
- Humphries, J.D. et al. (2007) J Cell Biol 179, 1043-57.
- Witt, S. et al. (2004) J Biol Chem 279, 31533-43.
- Xu, W. et al. (1998) Development 125, 327-37.
- Ziegler, W.H. et al. (2002) J Biol Chem 277, 7396-404.
- Zhang, Z. et al. (2004) Mol Biol Cell 15, 4234-47.
- Rodríguez Fernández, J.L. et al. (1993) J Cell Biol 122, 1285-94.
- Samuels, M. et al. (1993) J Cell Biol 121, 909-21.
- Yang, H.J. et al. (2010) Cancer Invest 28, 127-34.
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