VCL / Vinculin Protein (His Tag)

Vinculin Protein Datasheet

VCL / Vinculin Protein Product Information

• Synonym: RP11-178G16.3, CMD1W, CMH15, MVCL
• Protein Construction: A DNA sequence encoding the human VCL (P18206-2) (Met 1- Gln 1066) was expressed, fused with a polyhistidine tag at the C-terminus.
• Source: Human
• Expression Host: Human Cells

VCL / Vinculin Protein QC Testing

• Purity: > 90 % as determined by SDS-PAGE.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Met 1
• Molecular Mass: The recombinant human VCL consists of 1077 amino acids and has a calculated molecular mass of 118 KDa. The apparent molecular mass of rhVCL is approximately 115 KDa in SDS-PAGE under reducing conditions.
• Formulation: Lyophilized from sterile PBS , pH 7.4
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: VCL / Vinculin protein

VCL / Vinculin Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

VCL / Vinculin Protein Description

Vinculin (VCL), is a cytoskeletal protein that is closely related to both cell-matrix interactions and cell-cell junctions. VCL is a membrane-cytoskeletal protein in focal adhesion plaques that is involved in linkage of integrin adhesion molecules to the actin cytoskeleton. The protein contains an acidic N-terminal domain and a basic C-terminal domain separated by a proline-rich middle segment. This protein has multi-ligand properties and has been found to interact with a number of microfilament associated proteins, such as talin, a-actinin, paxillin and a-catenin, which reportedly bind to either the head or tail domains of vinculin. Moreover, it is believed that vinculin can serve as a dynamic link between the cytoskeleton and cell surface adhesion molecules, such as integrins and E-cadherins. Vinculin has also been implicated in the control of adhesion and motility of fibroblasts, PC12 cells and chick neuronal cells.

References

1. Massoumi R. et al., 2001, J Cell Sci. 114 (10): 1925-34.
2. Turner CE. et al., 1994, J Cell Sci. 107 (6): 1583-91.
3. Strasser P. et al., 1993, FEBS Lett. 317: 189-194.