Vinculin Antibody

• 产品编号：CST-4650S      品牌：CST       原厂货号：4650S
• 产品分类：抗体 > 一抗 > 蛋白特异性一抗
• 应用分类：

描述：

抗体检测内源性总Vinculin蛋白水平，此抗体也和Vinculin的剪接变异体145kDa的metavinculin反应。多抗由合成的肽段免疫动物产生，该合成肽段对应人Vinculin蛋白的N氨基末端附近残基。抗体由蛋白A和肽段亲和层析技术纯化。Vinculin是细胞骨架蛋白，在焦点粘着和胚胎发育中起重要作用（1-4）。三种结构的vinculin结构域包括一个N氨基末端头，一个短而弯曲的脯氨酸富集区和一个C末端尾巴（1）。在失活状态下，Vinculin头和尾结构域相互作用形成一个封闭的结构。开放并激活的Vinculin形式转位到焦点粘着，在那里被认为涉及锚定F-actin到胞膜上，并调控细胞迁移（2）。磷脂结合尾巴结构域，随后Vinculin被PKC-α磷酸化的1033位丝氨酸和1045位丝氨酸，被Src激酶磷酸化100位酪氨酸和1065位酪氨酸，使得头尾的相互作用减弱（5,6）。vinculin 的这种改变允许许多其他蛋白的结合，包括talin, α-actinin和 paxillin, 它们破坏头尾相互作用，起始从失活到激活状态的结构性变化（2,4）。Vinculin缺失与细胞粘附减少以及细胞移动增肌有关，暗示转移性增长的可能作用（7,8）。这一观点被近来结肠癌中减少的Vinculin表达和增加的致癌转移之间有关联所支持（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.

原厂资料：

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.

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.

注意事项：

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