Vinculin (E1E9V) Rabbit Monoclonal Antibody (HRP Conjugate)#18799,Cell Signaling Technology (CST),18799

Vinculin (E1E9V) Rabbit Monoclonal Antibody (HRP Conjugate) recognizes endogenous levels of total vinculin protein. This antibody conjugate also reacts with metavinculin, a 145 kDa splice variant of vinculin.

Host

Rabbit

Reactivity

Human, Mouse, Rat, Monkey

Application

Western Blotting: 1:1000

Platform ID

BAB270248363

Cell Signaling Technology (CST)

Headquarters

3 Trask Lane Danvers, MA 01923

Contact

Tel: 877-616-2355,978-867-2388
Fax: 877-616-2355

Product Specifications
Scientific Background
Synonyms

Specifications

NameVinculin (E1E9V) Rabbit Monoclonal Antibody (HRP Conjugate)#18799
Cat. No.18799
Accession NumberP18206
Gene ID (Entrez)18206, 7414
HostRabbit
SensitivityEndogenous
ReactivityHuman, Mouse, Rat, Monkey
ApplicationWestern Blotting: 1:1000
Molecular Weight124
ImmunogenIgG
FormulationSupplied in 136 mM NaCl, 2.6 mM KCl, 12 mM sodium phosphate (pH 7.4) dibasic, 2 mg/ml BSA, and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
StorageSupplied in 136 mM NaCl, 2.6 mM KCl, 12 mM sodium phosphate (pH 7.4) dibasic, 2 mg/ml BSA, and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Regulatory StatusResearch Use Only

Scientific 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).Izard, T. et al. (2004)Nature427, 171-5.Humphries, J.D. et al. (2007)J Cell Biol179, 1043-57.Witt, S. et al. (2004)J Biol Chem279, 31533-43.Xu, W. et al. (1998)Development125, 327-37.Ziegler, W.H. et al. (2002)J Biol Chem277, 7396-404.Zhang, Z. et al. (2004)Mol Biol Cell15, 4234-47.Rodríguez Fernández, J.L. et al. (1993)J Cell Biol122, 1285-94.Samuels, M. et al. (1993)J Cell Biol121, 909-21.Yang, H.J. et al. (2010)Cancer Invest28, 127-34.Alternate NamesCMD1W; CMH15; epididymis luminal protein 114; epididymis secretory sperm binding protein; HEL114; meta-vinculin; Metavinculin; MV; MVCL; VCL; VINC; Vinculin; Vinculin iso2

Synonyms

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

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