The Vimentin Antibody from MyBioSource.com is a Rabbit Polyclonal antibody to VIM, and Vimentin. This antibody recognizes Human, and Rat antigen. The Vimentin Antibody has been validated for the following applications: ELISA, Immunocytochemistry, Immunofluorescence, Immunohistochemistry, and Western Blot.
Description
Description: VIM is an intermediate filament protein. Intermediate filament proteins are expressed in a tissue-specific manner. Desmin is the subunit specific for muscle and vimentin the subunit specific for mesenchymal tissue.
Function: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.
Subunit Structure: Homopolymer assembled from elementary dimers. Interacts with HCV core protein (PubMed:15846844). Interacts with LGSN and SYNM. Interacts (via rod region) with PLEC (via CH 1 domain) (By similarity). Interacts with SLC6A4 (PubMed:19270731). Interacts with STK33 (PubMed:18811945). Interacts with LARP6 (PubMed:21746880). Interacts with RAB8B (By similarity). Interacts with TOR1A; the interaction associates TOR1A with the cytoskeleton (PubMed:16361107, PubMed:18827015). Interacts with TOR1AIP1 (PubMed:16361107). Interacts with BCAS3 (PubMed:17505058). Interacts with DIAPH1 (PubMed:23325789). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament (PubMed:16923132). Interacts with the non-receptor tyrosine kinase SRMS; the interaction leads to phosphorylation of VIM (PubMed:29496907).
Post-translational Modifications: Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as well as by nestin (By similarity). One of the most prominent phosphoproteins in various cells of mesenchymal origin. Phosphorylation is enhanced during cell division, at which time vimentin filaments are significantly reorganized. Phosphorylation by PKN1 inhibits the formation of filaments. Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm (PubMed:21465480). Phosphorylated by STK33 (PubMed:18811945). Phosphorylated on tyrosine residues by SRMS (PubMed:29496907). O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status. S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.
Similarity: The central alpha-helical coiled-coil IF rod domain mediates elementary homodimerization.The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex. Belongs to the intermediate filament family