V5255
Anti-Vimentin Antibody
mouse monoclonal, VIM-13.2
Synonyme(s) :
Anti-F5H288
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About This Item
Nom du produit
Monoclonal Anti-Vimentin antibody produced in mouse, clone VIM-13.2, ascites fluid
biological source
mouse
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
VIM-13.2, monoclonal
species reactivity
chicken, rat, human, rabbit, frog, mouse
technique(s)
indirect immunofluorescence: 1:200 using cultured chicken fibroblasts
western blot: 1:500 using human fibroblasts cell extract
isotype
IgM
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... VIM(7431)
mouse ... Vim(22352)
rat ... Vim(81818)
Application
Monoclonal anti-vimentin antibody can be used in the following:
- Immunocytochemical localization of vimentin in normal and pathological tissue of mesenchymal origin.
- It can also be used in immunoblotting
- Immunofluorescence
- Further, anti-vimentin antibody can be used to distinguish tumors and metastatic lesions derived from sarcomas, lymphomas, and melanomas.
Biochem/physiol Actions
Vimentin has a crucial role in maintaining cell shape and motility. It also provides mechanical stress tolerance for mesenchymal cells. Vimentin induces fibroblast motility and promotes wound healing process. Vimentin filaments form a part of cytoskeleton filament system and therefore, support and secure the cell organelles and also maintain cellular integrity. Vimentin is associated with the process of initiation, progression, metastasis and epithelial-mesenchymal transition of cancer cells, thereby contributing to tumorigenesis. Upregulation of this gene is observed in various cancers including prostate cancer, gastrointestinal tumors, lung cancer, breast cancer, CNS tumors and malignant melanoma.
Disclaimer
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.
General description
Vimentin is a 53 kD type III intermediate filaments expressed in breast myoepithelial cells, osteocytes, langerhans cells of the skin, schwann cells and astrocytes. Monoclonal anti-vimentin antibody can be used in immunofluorescent labeling of frozen tissue sections to localize vimentin in fibroblasts, endothelial cells, lymphoid tissues and melanocytes. It can also be used in western blotting. Mouse anti-vimentin antibody reacts specifically with vimentin. This product has also shown best reactivity with cultured chicken fibroblasts and can also react with human and mouse cells or tissues.The protein monomers consist of α-helical rod, flanked by head and tail domains. The VIM gene is mapped to human chromosome 10p13.
Immunogen
human foreskin fibroblasts
Other Notes
This product can be found as purified product that was produced using cell culture hybridoma product.
SAB4200716 Anti-Vimentin antibody, Mouse monoclonal
clone VIM-13.2, purified from hybridoma cell culture
SAB4200716 Anti-Vimentin antibody, Mouse monoclonal
clone VIM-13.2, purified from hybridoma cell culture
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Classe de stockage
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Lung cancer exosomes as drivers of epithelial mesenchymal transition.
Rahman M A, et al.
Oncotarget, 7(34), 54852-54852 (2016)
Yvonne Ting-Chun Yu et al.
Journal of biomedical science, 23, 14-14 (2016-01-24)
Severe acute respiratory syndrome coronavirus (SARS-CoV) caused a global panic due to its high morbidity and mortality during 2002 and 2003. Soon after the deadly disease outbreak, the angiotensin-converting enzyme 2 (ACE2) was identified as a functional cellular receptor in
A novel role of vimentin filaments; binding and stabilization of collagen mRNAs.
Challa A A and Stefanovic B
Molecular and Cellular Biology (2011)
Tine Van Bergen et al.
Journal of cellular and molecular medicine, 17(12), 1632-1643 (2013-10-15)
Excessive post-operative wound healing with subsequent scarring frequently leads to surgical failure of glaucoma filtration surgery (trabeculectomy). We investigated the hypothesis that placental growth factor (PlGF) plays a role in post-operative scar formation, and that it therefore may be a
Alba Jene-Sanz et al.
Molecular and cellular biology, 33(19), 3951-3961 (2013-08-07)
Global changes in the epigenome are increasingly being appreciated as key events in cancer progression. The pathogenic role of enhancer of zeste homolog 2 (EZH2) has been connected to its histone 3 lysine 27 (H3K27) methyltransferase activity and gene repression;
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