Recombinant Human Vimentin protein (Tagged-His Tag)
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(1 Publication)
Recombinant Human Vimentin protein (Tagged-His Tag) is a Human Full Length protein, in the 1 to 466 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, WB.
View Alternative Names
Vimentin, VIM
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Vimentin protein (Tagged-His Tag) (AB84704)
SDS-PAGE of ab84704 using 3ug Vimentin protein. Detected molecular weight approximately 60 kDa.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Specifications
Form
Liquid
Additional notes
Purity >95% as determined by densitometry.
General info
Function
Vimentin, a class-III intermediate filament, is present in various non-epithelial cells, particularly mesenchymal cells, and connects either laterally or terminally to the nucleus, endoplasmic reticulum, and mitochondria. It is involved with LARP6 in stabilizing type I collagen mRNAs for CO1A1 and CO1A2. This supplementary information is collated from multiple sources and compiled automatically.
Sequence similarities
Belongs to the intermediate filament family.
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.
Subcellular localisation
Cytoskeleton
Target data
Publications (1)
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The Journal of biological chemistry 289:6960-8 PubMed24474691
2014
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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