| Reactivity | Hu, Mu, RtSpecies Glossary |
| Applications | WB, Simple Western, IHC, Flow, ICC/IF, KO, mIF |
| Clone | 280618 |
| Clonality | Monoclonal |
| Host | Rat |
| Conjugate | Unconjugated |
| Concentration | LYOPH |
| Immunogen | E. coli-derived recombinant human Vimentin Ser2-Glu466 Accession # P08670 |
| Specificity | Vimentin antibodies are ideal for immunocytochemistry colocalization studies in intermediate filaments. Detects human, mouse and rat Vimentin in Western blots. |
| Source | N/A |
| Isotype | IgG2a |
| Clonality | Monoclonal |
| Host | Rat |
| Gene | VIM |
| Purity Statement | Protein A or G purified from hybridoma culture supernatant |
| Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
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| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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| Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. See Certificate of Analysis for details. *Small pack size (-SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS. |
| Preservative | No Preservative |
| Concentration | LYOPH |
| Reconstitution Instructions | Reconstitute at 0.5 mg/mL in sterile PBS. For liquid material, refer to CoA for concentration. |
Vimentin is a 57 kDa class III intermediate filament (IF) protein that belongs to the intermediate filament family. It is the predominant IF in cells of mesenchymal origin such as vascular endothelium and blood cells (1-3). The human Vimentin cDNA encodes a 466 amino acid (aa) protein that contains head and tail regions with multiple regulatory Ser/Thr phosphorylation sites, and a central rod domain with three coiled-coil regions separated by linkers (1, 2). Human Vimentin shares 97-98% aa identity with mouse, rat, ovine, bovine, and canine Vimentin. Sixteen Vimentin coiled-coil dimers self-assemble to form intermediate (10-12 nm wide) filaments (4). These filaments then anneal longitudinally to form non-polarized fibers that support cell structure and withstand stress (4). IF fibers are highly dynamic, and half-life depends on the balance between kinase and phosphatase activity. For example, phosphorylation followed by dephosphorylation drives IF disintegration, followed by reorganization during mitosis (1, 5, 6). Interactions of head and tail domains link IFs with other structures such as actin and microtubule cytoskeletons (7). Vimentin is involved in positioning autophagosomes, lysosomes and the Golgi complex within the cell (8). It facilitates cell migration and motility by recycling internalized trailing edge integrins back to the cell surface at the leading edge (9-11). Vimentin helps maintain the lipid composition of cellular membranes, and caspase cleavage of Vimentin is a key event in apoptosis (8, 12). Phosphorylation promotes secretion of Vimentin by TNF-alpha -stimulated macrophages (13). Extracellular Vimentin has been shown to associate with several microbes, and appears to promote an antimicrobial oxidative burst (13, 14). Cell-associated Vimentin can also interact with NKp46 to recruit NK cells to tuberculosis-infected monocytes (15).
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| Images | Ratings | Applications | Species | Date | Details | ||||||||
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reviewed by:
Sam Connell |
IHC-Fr | Human | 02/22/2019 |
Summary
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Secondary Antibodies |
Isotype Controls |
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Taking Biomarker Discovery From 2D to 3D: Increased Biological Activity of EVs Isolated From 3D Prostate Cancer Cultures Jamshed Arslan, Pharm D, PhD Tissues within the human body are made of a three-dimensional (3D) arrangement of cells working together to perform vital functions. The commonly used 2D monolayer cultures have limited ... Read full blog post. |
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Antibody treatment can generate microglia-like cells from bone marrow By Jennifer Sokolowski, MD, PhD.Microglia play important roles in the brain in both homeostatic and pathological conditions, acting to clear debris and dying cells. There is evidence to suggest that microglial dys... Read full blog post. |
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Stemness is responsible for onset and metastasis of colorectal cancer By Jamshed Arslan, Pharm. D., PhD. Colorectal cancer stem cells are a rare subpopulation of colorectal cancer cells that can self-renew and initiate and sustain tumor growth when transplanted into an animal host.1,2 C... Read full blog post. |
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The use of Beta Actin (AC-15) as a loading control across multiple species Actin is a fundamental component of the cytoskeleton, where it has the ability to create and break down actin filament formation in response to various cell needs. Actin has six highly conserved isoforms, however beta and gamma actin are the two... Read full blog post. |
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The use of actin as a loading control in research on fruiting-body development and vegetative growth in Sordaria macrospora research Sordaria macrospora is a filamentous fungus that serves as very useful system for scientific research due to a short life cycle and easy manipulation. Just like any other model organism, it is important to have an effective loading control to va... Read full blog post. |
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Alpha-smooth muscle actin and the modulation of endothelial and epithelial cell biology Actin is essential for a wide range of cell functions, ranging from cell division and chromatin remodeling to vesicle trafficking and maintenance of cellular structure. In fact, mislocalization of actin to cell junctions during development leads t... Read full blog post. |
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Epithelial-Mesenchymal Transition (EMT) Markers Epithelial-Mesenchymal Transition (EMT) is the trans-differentiation of stationary epithelial cells into motile mesenchymal cells. During EMT, epithelial cells lose their junctions and apical-basal polarity, reorganize their cytoskeleton, undergo a... Read full blog post. |
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CD63: is it pro-metastatic or anti-metastatic? CD63 is a type II membrane protein belonging to tetraspanin superfamily and it play key roles in the activation of several cellular signaling cascades along with acting as TIMP1 receptor. It is expressed by activated platelets, monocytes,... Read full blog post. |
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Vimentin: Regulating EMT and Cancer Vimentin, a member of the intermediate filament (IF) family, is a protein responsible for maintaining cellular integrity and reducing damage caused by stress. The vimentin protein is ubiquitously expressed in normal mesenchymal cells, and recent resea... Read full blog post. |
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![Widespread GLI expression in human donor and cirrhotic liver.(A) Frozen (4 μm) human donor (n = 5), and cirrhotic liver sections [ALD (n = 6), NASH (n = 3), PBC (n = 1)] were screened for GLI2 (red) expression by immunofluorescence. Representative images taken at 5x or 40x (insets) objective shown. DAPI, blue. (B) qRT-PCR for GLI1 and GLI3 transcript in human donor or ALD samples. Mean±S.E.M. Significant (*) difference between means (One-sided student t-test, **p150 kDa) in donor (Don) or ALD patient samples. Densitometry analysis with GLI1 normalised to GAPDH (Image J). Mean±S.E.M; **p = 0.0093 (Two-sided student t-test). (C) Nuclear GLI2 (green) expression in EpCAM+ (red) LPCs in donor, ALD, PBC and NASH liver. (D) Nuclear GLI2 (green) expression demonstrated within CD31+ (red) ECs, CK18+ (red) hepatocytes, CD45+ (red) leukocytes and vimentin+ (red) HSCs/myofibroblasts, in ALD. 63x objective. (E) Maximum intensity projection illustrating close physical association between EpCAM+ LPCs (green) and vimentin+ HSCs/myofibroblasts (red), both of which express GLI2 (grey), in ALD tissue. Arrows indicate myofibroblasts directly contacting LPCs. Confocal microscopy, 63x objective. Quantitation (%) of EpCAM+ GLI2+ cells and vimentin+ GLI2+ cells within the same FOV (n = 3 ALD samples, 8 FOV/sample). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0171480), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/mab2105_human-mouse-rat-vimentin-mab-clone-280618-41202410331991.jpg "Widespread GLI expression in human donor and cirrhotic liver.(A) Frozen (4 μm) human donor (n = 5), and cirrhotic liver sections [ALD (n = 6), NASH (n = 3), PBC (n = 1)] were screened for GLI2 (red) expression by immunofluorescence. Representative images taken at 5x or 40x (insets) objective shown. DAPI, blue. (B) qRT-PCR for GLI1 and GLI3 transcript in human donor or ALD samples. Mean±S.E.M. Significant (*) difference between means (One-sided student t-test, **p150 kDa) in donor (Don) or ALD patient samples. Densitometry analysis with GLI1 normalised to GAPDH (Image J). Mean±S.E.M; **p = 0.0093 (Two-sided student t-test). (C) Nuclear GLI2 (green) expression in EpCAM+ (red) LPCs in donor, ALD, PBC and NASH liver. (D) Nuclear GLI2 (green) expression demonstrated within CD31+ (red) ECs, CK18+ (red) hepatocytes, CD45+ (red) leukocytes and vimentin+ (red) HSCs/myofibroblasts, in ALD. 63x objective. (E) Maximum intensity projection illustrating close physical association between EpCAM+ LPCs (green) and vimentin+ HSCs/myofibroblasts (red), both of which express GLI2 (grey), in ALD tissue. Arrows indicate myofibroblasts directly contacting LPCs. Confocal microscopy, 63x objective. Quantitation (%) of EpCAM+ GLI2+ cells and vimentin+ GLI2+ cells within the same FOV (n = 3 ALD samples, 8 FOV/sample). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0171480), licensed under a CC-BY license. Not internally tested by R&D Systems.")
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