Description_x000D_ General description_x000D_ Monoclonal Anti-Plectin (mouse IgG1 isotype) is derived from the 7A8 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. Plectin is an abundant, high molecular weight, cytomatrix protein (300 kDa) found in a wide variety of tissue and cell types. Plectin is found in stratified and non-stratified epithelia, fibroblasts, endothelial cells and astrocytes, as well as in striated, smooth and cardiac muscle, but not in neurons._x000D_ Specificity_x000D_ The antibody recognizes an epitope located in the middle section of the rod domain of the plectin molecule, approximately halfway between the globular end domains. The kinase C phosphorylation site was found on the same terminal segment as this antibody epitope. The antibody specifically labels the 300 kDa band of plectin, however, lower M.W. band(s) may also be detected. The antibody stains filamentous structures on immunohistochemical staining of frozen tissue sections. The antibody inhibits the interaction of plectin with vimentin and lamin B. An additional application for this antibody is immunoelectronmicroscropy._x000D_ Immunogen_x000D_ plectin from rat glioma C6 cells_x000D_ Application_x000D_ Monoclonal Anti-Plectin antibody produced in mouse has been used in:_x000D_ • ELISA_x000D_ • immunoblot_x000D_ • dot blot_x000D_ • immunocytochemistry_x000D_ • immunoelectron microscopy_x000D_ Disclaimer_x000D_ Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals._x000D_ Biochem/physiol Actions_x000D_ Plectin plays a role in the cross-linking of intermediate filaments, the interlinking of intermediate filaments with microtubules and microfilaments and the anchoring of intermediate filaments to the plasma membrane and the nuclear membrane. It is a part of the signal transduction mechanism involving kinases A and C, because in vitro as well as in vivo phosphorylation of the protein by those kinases differentially affected its binding affinities to vimentin and lamin B.