Vinculin, a cytoskeletal protein, plays an important role during embryonic development and focal adhesion regulation (1-4). There are three domains of structural vinculin: an amino-terminal head and a proline-rich, short region, and a carboxy terminal tail. The closed confirmation is formed when the head domain and tail domains interact in the inactive state. 

Vinculin's active and open form translocates to focal adhesions, where it is believed to play a role in the anchoring of F-actin to membrane and regulation cell migration. Phospholipid binding at the tail domain and subsequent PKC-a and Tyr100/Tyr1065 phosphorylation weakens the head/tail interaction. You can know more about Vinculin/VCL antibody A01207-1 online.

This alteration in vinculin permits the binding of a variety of proteins, such as talin, a–actinin, and paxillin. This disrupts the head–tail interaction and initiates a conformational change, from the inactive state to the active. Vinculin deficiencies can lead to a decrease of cell adhesion and increased cell motility. This could be a role in metastatic growth. 

This conclusion is supported by the evidence linking decreased vinculin expression with increased carcinogenesis and metastasis of colorectal carcinoma. Vinculin Antibody (H-10) is a mouse monoclonalIgG 2a K, cited in 121 publications. It can be found at 200/ml

Anti-Vinculin antibody Mouse monoclonal (mouse IgG1 type) is derived by the VIN-11-5 hybridoma, which is the result of the fusion between mouse myeloma cell and splenocytes derived from a mouse that was immunized using smooth muscle vinculin from the chicken gizzard.