Invitrogen™ Vimentin Monoclonal Antibody (V9), eBioscience™, Invitrogen™

Description

Description: The V9 monoclonal antibody recognizes human Vimentin, a 57 kDa protein that functions as a structural component of intermediate filaments. Vimentin is expressed in cells derived from the mesenchyme but also in specific populations such as radial glia and immature glial cells, pancreatic precursor cells. It is proposed to be a marker of cardiac differentiation. In neural cells, vimentin expression is gradually replaced by neurofilaments. Reports have also shown surface expression of vimentin on activated macrophages, platelets, as well as apoptotic T cells and neutrophils. This antibody also recognizes canine (dog), rat and chicken vimentin but does not recognize mouse vimentin. Applications Reported: This V9 antibody has been reported for use in western blotting, immunocytochemistry, and immunohistochemical staining of frozen (IHC-F) and formalin-fixed paraffin embedded tissue sections (IHC-P). Applications Tested: This V9 antibody has been tested by immunocytochemistry on paraformaldehyde fixed and permeabilized SK-N-SH or C6 cell lines and by western blot on cell lysates prepared from HeLa cells. This antibody can be used at less than or equal to 1 μg/mL. It is recommended that this antibody be carefully titrated for optimal performance in the assay of interest. Purity: Greater than 90%, as determined by SDS-PAGE. Aggregation: Less than 10%, as determined by HPLC. Filtration: 0.2 μm post-manufacturing filtered.

Vimentin is a developmentally regulated intermediate filament protein (IFP) found in cells of mesenchymal origin. It is believed to be involved with the intracellular transport of proteins between the nucleus and plasma membrane. Unlike other IFP proteins, vimentin is expressed, along with desmin, during the early stages of cellular development. During the development process, vimentin is exchanged for new, tissue-specific IFPs. Vimentin has been implicated to be involved in the rate of steroid synthesis via its role as a storage network for steroidogenic cholesterol containing lipid droplets. Vimentin phosphorylation by a protein kinase causes the breakdown of intermediate filaments and activation of an ATP and myosin light chain dependent contractile event. This results in cytoskeletal changes that facilitate the interaction of the lipid droplets within mitochondria, and subsequent transport of cholesterol to the organelles leading to an increase in steroid synthesis.