Cell Signaling Technology

Product Pathways - Adhesion

Vinculin (E1E9V) XP® Rabbit mAb (HRP Conjugate) #18799

No. Size Price
18799S 100 µl ( 10 western blots ) ¥4,264.00 现货查询 购买询价
18799 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Rat,Monkey, Endogenous 124 Rabbit IgG

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting,

Specificity / Sensitivity

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

Source / Purification

Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the amino terminus of human vinculin protein.

Description

This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Vinculin (E1E9V) XP® Rabbit mAb #13901.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa, PC-12 and Jurkat cells using Vinculin (E1E9V) XP® Rabbit mAb (HRP Conjugate).

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).

  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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Protocols

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

Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.

XP is a registered trademark of Cell Signaling Technology, Inc.

Tween is a registered trademark of ICI Americas, Inc.

Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.

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