|Immunogen:||Recombinant fusion protein containing a sequence corresponding to amino acids 767-1066 of human Vinculin.|
|Reactivity:||Hu, Ms, Rt|
Western Blot: 1:500-1:1000
Vinculin is a protein encoded by the VCL gene which is approximately 123,7 kDa. Vinculin is localised to the cell membrane. It is involved in RET signalling, signalling by moderate kinase activity BRAF mutants and focal adhesion. It is a cytoskeletal protein associated with cell-cell and cell-matrix junctions, where it is thought to function as one of several interacting proteins involved in anchoring F-actin to the membrane. It may also play important roles in cell morphology and locomotion. Vinculin is expressed in the muscles. Mutations in the VCL gene may result in cardiomyopathy. AB-81457 was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen. This polyclonal antibody detects endogenous levels of Vinculin protein. Specificity: Vinculin Polyclonal Antibody detects endogenous levels of Vinculin protein.
|Buffer:||PBS with 0.02% sodium azide and 50% glycerol pH 7.3|
|Storage:||Store at -20°C, and avoid repeat freeze-thaw cycles.|
Western Blot (WB) analysis of specific cells using Vinculin polyclonal antibody
Western Blot on Human breast cancer, using antibody at
Sample: Human breast cancer
Loading: 15 ug
Incubation time: over night at 4 ℃
IHC (p) on Human Skeletal Muscle
IHC short protocol
Antibody Name Anti-Vinculin Antibody
Primary Dilution 1:100
Primary Probing incubated for 1 hour.
Secondary Antibody DAB
Reference Antibody N/A
Secondary Dilution 1:200
Secondary Probing 33 minutes and then washed for 2 hours using PBS
Tissue Skeletal muscle
Tissue Processing overnight at room temperature (23°C).
Positive Control N/A
Negative Control N/A
Antigen Retrieval left overnight in -80°C freezer.
Blocking 5 hours with multiple changes of PBS
Wash •1 hour with at least 3 changes of PBS.
Visualization •The sample was then dehydrated and mounted in entellan.
Findings Immunohistochemical investigation showed increased vinculin immunoreactivity (also at the sarcolemm) in degenerating myofibres which is in accordance with our proteomic in vitro data and with the predicted subcellular localization of this protein.