| Weight | 1 lbs |
|---|---|
| Dimensions | 9 × 5 × 2 in |
| host | mouse |
| isotype | IgG1 |
| clonality | monoclonal |
| concentration | 1 mg/mL |
| applications | ICC/IF, IHC, WB |
| available sizes | 1 mg, 100 µg, 25 µg |
mouse anti-Vimentin monoclonal antibody (2A52) 8874
$100.00 – $2,600.00
Antibody summary
- Mouse monoclonal to Vimentin
- Suitable for: WB, ICC/IF, IHC
- Reacts with: human, rat
- Isotype: IgG1
- 100 µg, 25 µg, 1 mg
mouse anti-Vimentin monoclonal antibody (2A52) 8874
| target relevance |
|---|
| Vimentin, a key protein constituent of the intermediate filament cytoskeleton, plays a pivotal role in maintaining cellular integrity and structure. In research, vimentin has become a valuable biomarker due to its tissue-specific expression and involvement in various cellular processes. Immunohistochemical analysis of vimentin has been extensively utilized to identify and characterize mesenchymal cells, such as fibroblasts, endothelial cells, and immune cells, aiding in the study of tissue development, wound healing, and cancer progression. Additionally, vimentin has been linked to epithelial-mesenchymal transition (EMT), a critical process implicated in embryonic development and metastasis. Furthermore, efforts to develop vimentin-targeting therapies for cancer treatment have shown promise, as vimentin's involvement in EMT and tumor progression make it a potential therapeutic target for limiting cancer metastasis. Click for more on: cell markers and Vimentin |
| Protein names Vimentin |
| Gene names VIM,VIM |
| Protein family Intermediate filament family |
| Mass 53652Da |
| 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. ; Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. |
| Subellular location Cytoplasm Cytoplasm, cytoskeleton Nucleus matrix Cell membrane |
| Tissues Highly expressed in fibroblasts, some expression in T- and B-lymphocytes, and little or no expression in Burkitt's lymphoma cell lines. Expressed in many hormone-independent mammary carcinoma cell lines. |
| Structure Homomer assembled from elementary dimers (PubMed:20176112). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Interacts with BCAS3 (PubMed:17505058). Interacts with LGSN (By similarity). Interacts with SYNM (By similarity). Interacts (via rod region) with PLEC (via CH 1 domain) (By similarity). Interacts with PLEC isoform 1C (PubMed:24940650). 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 DIAPH1 (PubMed:23325789). 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). Interacts with NOD2 (PubMed:27812135). Interacts (via head region) with CORO1C (By similarity). Interacts with HDGF (isoform 2) (PubMed:26845719). Interacts with PRKCE (via phorbol-ester/DAG-type 2 domain) (PubMed:18408015). Interacts with BFSP2 (By similarity). Interacts with PPL (By similarity). Interacts (via rod domain) with PKP1 (PubMed:10852826). Interacts with PKP2 (PubMed:10852826). ; (Microbial infection) Interacts with HCV core protein. |
| Post-translational modification 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. |
| Target Relevance information above includes information from UniProt accession : P08670 |
| The UniProt Consortium |
Data
 |
| Immunofluorescent analysis of cortical neuron-glial cell culture from E20 rat stained with mouse mAb to vimentin, 36822, dilution 1:5,000 in green, and costained with rabbit pAb to glial fibrillary acidic protein (GFAP), 2539, dilution 1:5,000 in red. The blue is DAPI staining of nuclear DNA. Fibroblastic, microglial and developing astrocytic cells contain only vimentin, and so appear green. Maturing astrocytic cells contain variable amounts of GFAP and vimentin, and so may appear red or yellow. |
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| Chromogenic immunostaining of a 4% PFA fixed paraffin embedded rat kidney section with mouse mAb to vimentin, 36822, dilution 1:2,000, detected in DAB (brown) using the Vector Labs ImmPRESS method and reagents with citra buffer retrieval. Hematoxylin (blue) was used as the counterstain. The 36822 antibody labels tubular epithelium in kidney. This antibody performs well in testing with both 4% PFA and standard NBF fixed tissues but does not stain long term NBF fixed tissue effectively.Mouse select image for larger view.We recently found that this antibody, an IgG1 and 666, an IgG2a, both failed to bind mouse tissues although they work well on human, rat and many other species. This allowed us to firmly map the epitope for both antibodies to the peptide SRISLPLPNFSSLNREL, amino acids 409-425 of the human sequence. This peptide is located at the beginning of the non-helical “tail” region of the molecule and the peptide is totally conserved in most mammalian species including, besides human and rat, cow, pig, horse, camel and many monkeys. These findings increase the general utility of these reagents. A sequence alignment of the human, rat and mouse vimentin sequences can be downloaded here. |
 |
| Western blot analysis of cell and whole brain tissue lysates using mouse mAb to vimentin, 36822, dilution 1:5,000 in green: [1] protein standard (red), [2] HEK293, [3] HeLa, [4] SH-SY5Y, [5] COS-1, [6] C6, and [7] rat brain. The band at about 50kDa mark corresponds to vimentin protein. The antibody does not recognize mouse vimentin (not shown). |
Publications
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.There are 7 publications in our database for this antibody or clone. Here are the latest 5, for more click below.
| pmid | title | authors | citation |
|---|---|---|---|
| 28450710 | Targeted Exome Sequencing of Congenital Cataracts Related Genes: Broadening the Mutation Spectrum and Genotype-Phenotype Correlations in 27 Chinese Han Families | Zhai Y, Li J, Yu W, Zhu S, Yu Y, Wu M, Sun G, Gong X, Yao K. | Sci Rep. 2017 Apr 27;7(1):1219. doi: 10.1038/s41598-017-01182-9. |
| 25187410 | Vimentin-a potential biomarker for therapeutic efficiency of HAART | Jia X, Liu L, Liu X, Wu D, Yin L, Liu X, Zhang J, Yang P, Lu H, Zhang L. | Acta Biochim Biophys Sin (Shanghai). 2014 Nov;46(11):1001-6. doi: 10.1093/abbs/gmu075. Epub 2014 Sep 3. |
| 22903723 | Discovery of lamin B1 and vimentin as circulating biomarkers for early hepatocellular carcinoma | Wong KF, Luk JM. | Methods Mol Biol. 2012;909:295-310. doi: 10.1007/978-1-61779-959-4_19. |
| 21637948 | Vimentin in cancer and its potential as a molecular target for cancer therapy | Satelli A, Li S. | Cell Mol Life Sci. 2011 Sep;68(18):3033-46. doi: 10.1007/s00018-011-0735-1. Epub 2011 Jun 3. |
| 19126778 | Dominant cataract formation in association with a vimentin assembly disrupting mutation | Müller M, Bhattacharya SS, Moore T, Prescott Q, Wedig T, Herrmann H, Magin TM. | Hum Mol Genet. 2009 Mar 15;18(6):1052-7. doi: 10.1093/hmg/ddn440. Epub 2009 Jan 6. |
Protocols
| relevant to this product |
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| Western blot IHC ICC |
Documents
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