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Human VCL / Vinculin Protein (His Tag)

CMD1W,CMH15,HEL114,MV,MVCL

Catalog Number P10019-H08H
Organism Species Human
Host Human Cells
Synonyms CMD1W,CMH15,HEL114,MV,MVCL
Molecular Weight 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.
predicted N Met 1
SDS-PAGE
Purity > 90 % as determined by SDS-PAGE
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.
Bio-activity
Research Area Cancer |Signal transduction |Akt Pathway |Phospholipases, Small GTPases, and Other Molecules in the Akt Pathway
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.
Background 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, and paxillin, which reportedly bind to either the head or tail domains of vinculin.
Reference
  • Massoumi R, et al. (2001) Leukotriene D(4) affects localisation of vinculin in intestinal epithelial cells via distinct tyrosine kinase and protein kinase C controlled events. J Cell Sci. 114(10): 1925-34.
  • Turner CE, et al. (1994) Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: identification of a vinculin and pp125Fak-binding region. J Cell Sci. 107 (6): 1583-91.
  • Strasser P, et al. (1993) Variable and constant regions in the C-terminus of vinculin and metavinculin: cloning and expression of fragments in E. coli. FEBS Lett. 317: 189-194.