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Vimentin

Vimentin is a type III intermediate filament protein that is widely expressed in various cell types, particularly in cells of mesenchymal origin.
It plays a crucial role in maintaining the structural integrity of cells, and its expression is often used as a marker for epithelial-to-mesenchymal transition (EMT) and cancer metastasis.
Vimentin is involved in a variety of cellular processes, including cell migration, adhesion, and signaling.
Researchers studying Vimetin can leverage PubCompare.ai's AI-driven protocol comparison to optimize their experiments, locate the best protocols, and identify the most reproducible solutions for their Vimetin research.
This tool can enhance scientific reproducibility and drive breakthroughs in the understanding of Vimetin's function and its role in disease.

Most cited protocols related to «Vimentin»

1
Mammalian Expression Plasmid Construction
Cited 28 times
To construct mammalian expression plasmids, the respective genes of FPs were PCR-amplified as AgeI-NotI fragments and swapped with a gene encoding EGFP in the pEGFP-N1 plasmid (Clontech). IFP2.0-N1 and mIFP-N1 plasmids were acquired from Addgene (#54785 and #54620, respectively).
For protein tagging and labelling of intracellular structures study, miRFPs were amplified, digested with restriction enzymes and then swapped with mTagBFP2 either as C- (for α-tubulin and clathrin) or N-terminal fusions (for keratin, α-actinin, LifeAct, EB3, myosin, vimentin, clathrin, LAMP1, zyxin, H2B and mitochondrial signal) as previously described50 (link). C-terminal fusions (SGGGG)n linker was increased to 30 amino acids. N-terminal fusions linker length was left unchanged.
To create an IκBα reporter plasmid (CMV-IκBα-miRFP703), we used a CMV-IκBα-FLuc plasmid kindly provided by S. Achilefu and D. Piwnica-Worms. A FLuc gene was replaced with one of the miRFP genes. Kozak sequence was deleted in the CMV-IκBα-miRFP703 and CMV-miRFP control plasmids.
miSplit670 and miSplit709 reporter plasmids, which are pC4-RHE-PAS, pC4EN-F1-mGAF670 and pC4EN-F1-mGAF709, were constructed from an iSplit plasmids25 (link) by swapping either PAS or GAF domains. A linker -ggggsggggs- was left unchanged. Where appropriate, an NLS sequence in the pC4EN-F1 plasmid was deleted by site-directed mutagenesis.
For mRNA labelling, a CMV-PAS-MCP plasmid was constructed as follows. PAS-ggggsggggs- without STOP codon was amplified as a single fragment and inserted into the C1 vector backbone using AgeI and KpnI sites, MCP was amplified from an ubc-nls-ha-MCP-VenusN-nls-ha-PCP-VenusC plasmid (Addgene, #52985) and inserted at KpnI and BamHI sites. The cmv-PCP-mGAF670 and cmv-PCP-mGAF709 plasmids were constructed as follows. A PCP without STOP codon was amplified from an ubc-nls-ha-MCP-VenusN-nls-ha-PCP-VenusC plasmid and then inserted into the C1 vector backbone using AgeI and EcoRI restriction sites. A -ggggsggggs-miGAF was amplified as a single fragment and inserted using EcoRI and KpnI sites. A phage-cmv-cfp-12xMBS-PBS was obtained by swapping a 12xMBS-PBS fragment from a Pcr4-12xMBS-PBS (Addgene, #52984) with 24xMS2 in a phage-cmv-cfp-24xms2 plasmid (Addgene, #40651). An ubc-nls-ha-MCP-VenusN-nls-ha-PCP-VenusC, a phage-cmv-cfp-24xMS2 and a Pcr4-12xMBS-PBS plasmids were gifts from B. Wu and R. Singer.
Plasmids encoding several green-red Fucci cell cycle reporters were provided by A. Miyawaki. The mKO2 and mAG genes fused with hCdt1(30–120), hCdt1(1/100), hGem(1/110) and hGem(1/60) sequences in the pCSII-EF-MCS plasmids were swapped with the miRFP709 or miRFP670v1 genes.
Shcherbakova D.M., Baloban M., Emelyanov A.V., Brenowitz M., Guo P, & Verkhusha V.V. (2016). Bright monomeric near-infrared fluorescent proteins as tags and biosensors for multiscale imaging. Nature Communications, 7, 12405.
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Publication 2016
Actinin alpha, NF-KappaB Inhibitor alpha-Tubulin Amino Acids Bacteriophages Cell Cycle Clathrin Cloning Vectors Codon, Terminator Cytokeratin Deoxyribonuclease EcoRI DNA Restriction Enzymes Genes Gifts Helminths lysosomal-associated membrane protein 1, human Mammals Mitochondria Mutagenesis, Site-Directed Myosin ATPase Plasmids Proteins Protoplasm RNA, Messenger Singer Vertebral Column Vimentin ZYX protein, human
2
Protein Extraction and Western Blot Analysis
Cited 19 times
Cells and tissues were lysed in RIPA buffer. Tumors were ground in liquid nitrogen and lysed. Protein concentration was determined using the BCA Kit (Beyotime Institute of Biotechnology). Proteins were mixed with loading buffer and heated at 70°C for 10 minutes on sodium dodecyl sulfate (SDS)-polyacrylamide gels at 30 μg per lane. The proteins were transferred to polyvinylidene fluoride (PVDF, Millipore, MA, USA) after electrophoresis. Membranes were blocked for 2 hours in 5% BSA and incubated overnight at 4°C with antibodies against γ-H2AX, ATM, ATR, Chk1, cell-cycle controller-2 (Cdc2), E-cadherin, vimentin, caspase-3, and caveolin-1 (Cav-1). The blots were then incubated with HRP-conjugated secondary antibody (1:1000; Santa Cruz Biotechnology). Finally, bands were visualized by enhanced chemiluminescence (Thermo Scientific Pierce, IL, USA).
Tian Y., Xie Q., He J., Luo X., Zhou T., Liu Y., Huang Z., Tian Y., Sun D, & Yao K. (2015). Radioactive 125I seeds inhibit cell growth and epithelial-mesenchymal transition in human glioblastoma multiforme via a ROS-mediated signaling pathway. BMC Cancer, 15, 1.
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Publication 2015
Antibodies Buffers Caspase 3 Caveolin 1 Cell Cycle Cells Chemiluminescence E-Cadherin Electrophoresis Immunoglobulins Neoplasms Nitrogen polyacrylamide gels polyvinylidene fluoride Proteins Radioimmunoprecipitation Assay Sulfate, Sodium Dodecyl Tissue, Membrane Tissues Vimentin
3
Optimizing CTC Isolation and Characterization
Cited 19 times
Eighteen samples (10 samples from NSCLC patients and 8 samples from breast cancer patients) were used to compare the efficacy of the CanPatrol CTC enrichment technique before and after optimization. For each sample, 5 ml of blood was used for CTC isolation and characterization using each method. Before optimization, a combination of the CD45+ magnetic bead separation and filtration methods was used for CTC isolation, and an immunostaining method was applied for CTC characterization. The protocol of this method has been described before [23 ]. To classify CTCs using EMT biomarkers, an antibody cocktail consisting of anti-EpCAM (R&D, Minneapolis, USA), anti-CK8/18/19 (R&D, Minneapolis, USA), anti-vimentin (BD Bioscience, San Jose, USA), anti-twist (BD Bioscience, San Jose, USA) and anti-CD45 (Surexam, Guangzhou, China) was used to stain the CTCs.
Wu S., Liu S., Liu Z., Huang J., Pu X., Li J., Yang D., Deng H., Yang N, & Xu J. (2015). Classification of Circulating Tumor Cells by Epithelial-Mesenchymal Transition Markers. PLoS ONE, 10(4), e0123976.
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Publication 2015
Biological Markers BLOOD Combined Antibody Therapeutics Filtration isolation Malignant Neoplasm of Breast Non-Small Cell Lung Carcinoma Patients Stains TACSTD1 protein, human Vimentin
4
Immortalized Human Mammary Epithelial Cells
Cited 16 times
Immortalized human mammary epithelial cells (HMLE) and V12H-Ras transformed derivatives (HMLER), including cells expressing empty vector (pWZL), Snail, Twist, Goosecoid (GSC) or an activated form of TGF-β1 were maintained as previously described (8 (link)). Established human breast cancer cell lines were cultured in cell specific medium as outlined in the SI Materials and Methods. Antibodies used included; anti-β-actin (Abcam), FOXC2 (Dr. Naoyuki Miura), E-cadherin (BD Bioscience), Fibronectin (BD Bioscience), N-cadherin (BD Bioscience), Vimentin (NeoMarkers) and β-catenin (BD Bioscience).
Hollier B.G., Tinnirello A.A., Werden S.J., Evans K.W., Taube J.H., Sarkar T.R., Sphyris N., Shariati M., Kumar S.V., Battula V.L., Herschkowitz J.I., Guerra R., Chang J.T., Miura N., Rosen J.M, & Mani S.A. (2013). FOXC2 expression links epithelial-mesenchymal transition and stem cell properties in breast cancer. Cancer research, 73(6), 1981-1992.
Publication 2013
Actins Antibodies Breast Cells Cloning Vectors CTNNB1 protein, human derivatives E-Cadherin Epithelial Cells FN1 protein, human Helix (Snails) Homo sapiens MCF-7 Cells N-Cadherins TGF-beta1 Vimentin
5
Quantitative 3D Tissue Imaging and Analysis
Cited 13 times
After preprocessing, we segmented all major tissue components. Images were converted into binary images by applying histogram-based threshold. For this purpose, the mode and standard deviation (σ) were determined for each channel of an image stack. Threshold levels were set to mode+σ for the WGA channel and mode+2σ for the DAPI, vimentin and α-SMA channels. We used a lower weighting factor for σ to threshold WGA channels because the high ratio of voxels with WGA signal (≥ 20%) led to a relatively higher standard deviation versus other channels. Images were then filtered with a binary median filter (radius 1). The segmented WGA signal was used to segment each cardiomyocyte by means of a watershed-based method as described previously.34 This method created labeled segments for each volume enclosed by WGA signal. At first, we identified myocytes. Subsequently, vessel lumens were identified within the non-myocyte segments. Vessel lumens were then dilated with a radius of 1 μm to include the vessel walls and endothelium. Possible overlap with the myocyte space was subtracted after the dilation. Cardiomyocyte and vessel volumes were then subtracted from the segmented WGA, DAPI, vimentin and α-SMA volumes. The remaining DAPI was identified as non-cardiomyocyte nuclei and merged with the remaining vimentin and α-SMA volumes. Using distance maps, we classified voxels of the merged volume closer to vimentin than to α-SMA as fibroblasts, while other voxels were classified as myofibroblasts. Finally, remaining non-classified segments from the watershed algorithm were merged with the remaining WGA volume and classified as extracellular space.
We determined volume ratios of all tissue components. Also, we calculated the number of neighboring myocytes by selecting complete cardiomyocytes, which were not truncated at image borders. We generated distance maps from the complete myocytes and then identified and counted all myocytes within a distance of 0.5 μm to the outer sarcolemma.
For 2D visualizations of images we used customized software. For 3D visualizations we applied Paraview (Kitware, Clifton Park, New York, USA), VolView (Kitware) and customized software.
Seidel T., Edelmann J.C, & Sachse F.B. (2015). Analyzing Remodeling of Cardiac Tissue: A Comprehensive Approach Based on Confocal Microscopy and 3D Reconstructions. Annals of biomedical engineering, 44(5), 1436-1448.
Publication 2015
A-factor (Streptomyces) Blood Vessel Cell Nucleus DAPI Dilatation Endothelium Extracellular Space factor A Fibroblasts Microtubule-Associated Proteins Muscle Cells Myocytes, Cardiac Myofibroblasts Radius Sarcolemma Tissues Vimentin

Most recents protocols related to «Vimentin»

1
Micropeptide Regulates Cancer Invasion
Not available on PMC !

Example 4

Given the effect of the overexpression of the SEQ ID NO:1, further experiments were performed to study its effect in cell invasion, another key oncogenic trait. Boyden chamber assay was used to determine invasiveness of A549 and H10 cancer cells after 4 days of doxycycline induction of SEQ ID NO:1, showing that the expression of the micropeptide induces a significant decrease in invasion (FIGS. 9A and B). In line with this observation, overexpression of the micropeptide of SEQ ID NO: 1 represses the expression of the EMT regulators VIMENTIN, SLUG, SNAIL, N-CADHERIN, TWIST1, TWIST2, ZEB1 and ZEB2 in H10 SCC cell line (FIG. 9C). This downregulation of the mesenchymal program further validates the role of the micropeptide of SEQ ID NO: 1 as a tumor suppressor.

US11858972B2. Micropeptides and uses thereof (2024-01-02). FUNDACIÓ PRIVADA INSTITUT D'INVESTIGACIÓ ONCOLÒGICA DE VALL HEBRON [ES]. Inventors: Maria Abad Méndez [ES], Olga Boix Sánchez [ES], Emanuela Greco [ES], Iñaki Merino Valverde [ES].
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Patent 2024
Biological Assay Carcinogenesis Cell Lines Cells Down-Regulation Doxycycline Mesenchyma N-Cadherins Neoplastic Cell Transformation Slugs Snails Tumor Suppressor Genes TWIST1 protein, human Vimentin
2
Prdm16 Regulates Pancreatic Cancer Progression
Fig. S1 shows that Prdm16 is transiently expressed in the premalignant lesions. Fig. S2 shows that Prdm16KO mice display normal insulin and glucagon expression and distribution as well as normal blood glucose levels. Fig. S3 provides additional data demonstrating that inactivation of Prdm16 accelerates KrasG12D-driven PDAC. Fig. S4 displays that Prdm16 is required for IPMN-to-PDAC progression and that Prdm16 deletion led to the accumulation of cells with high vimentin expression. In addition, Fig. S4 shows the effects of deleting PRDM16 on the proliferation of PANC-1 and BxPC-3 cell lines. Fig. S5 further expands upon the notion that concomitant inactivation of Prdm16 and Smad4 mimics the phenotype of complete TGF-β signaling inactivation through TβRII ablation.
Hurwitz E., Parajuli P., Ozkan S., Prunier C., Nguyen T.L., Campbell D., Friend C., Bryan A.A., Lu T.X., Smith S.C., Razzaque M.S., Xu K, & Atfi A. (2023). Antagonism between Prdm16 and Smad4 specifies the trajectory and progression of pancreatic cancer. The Journal of Cell Biology, 222(4), e202203036.
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Publication 2023
Anophthalmia with pulmonary hypoplasia Blood Glucose Cell Lines Cells Deletion Mutation Disease Progression Glucagon Insulin MEL1S protein, human Mus Phenotype Precancerous Conditions SMAD4 protein, human TGFBR2 protein, human Transforming Growth Factor beta Vimentin
3
Protein Characterization Using Antibodies
Chromatin immunoprecipitation (ChIP), immunoblotting, immunofluorescence, or immunohistochemistry were performed using the following antibodies: anti-α-SMA (#19245T; Cell Signaling); anti-β-Actin (#64225332; Bio-Rad), anti-amylase (#ab21156; Abcam), anti-chromogranin-A (#ab45179; Abcam), anti-cytokeratin 19 (#ab52625; Abcam), anti-E-cadherin (#3195S; Cell Signaling), anti-glucagon (#2760; Cell Signaling), anti-insulin (#4590; Cell Signaling), anti-JunB (#3753; Cell Signaling), anti-Muc5AC (#ab3649; Abcam), anti-Prdm16 (#ab202344 and #ab106410; Abcam), anti-Smad2 (#5339; Cell Signaling), anti-Smad3, (#9523; Cell Signaling), anti-Smad4, (#46535; Cell Signaling), anti-Smad4 (#sc-7966; Santa Cruz), anti-Smad2/3 (#8685; Cell Signaling), and anti-vimentin (#5741S; Cell Signaling).
Hurwitz E., Parajuli P., Ozkan S., Prunier C., Nguyen T.L., Campbell D., Friend C., Bryan A.A., Lu T.X., Smith S.C., Razzaque M.S., Xu K, & Atfi A. (2023). Antagonism between Prdm16 and Smad4 specifies the trajectory and progression of pancreatic cancer. The Journal of Cell Biology, 222(4), e202203036.
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Publication 2023
Actins Amylase Antibodies Cadherins Chromogranin A Glucagon Immunofluorescence Immunohistochemistry Immunoprecipitation, Chromatin Insulin Keratin-19 MEL1S protein, human MUC5AC protein, human SMAD2 protein, human SMAD3 protein, human SMAD4 protein, human Vimentin
4
Isolation and Culture of Human Decidual Stromal Cells
Primary HDSCs were separated from decidual tissues by means of enzymatic dispersion and mechanical dissociation, as mentioned before (Zhu et al., 2007 (link)). Generally, the samples were washed in cold phosphate-buffered saline (Gibco, Life Technologies, Inc., Carlsbad, CA, United States of America) three times, and then minced and treated with 0.1% collagenase (type IV; Sigma‒Aldrich), 0.1% hyaluronidase (type I-S; Sigma‒Aldrich) and 0.5 mg/ml DNase I (Sigma‒Aldrich) and subsequently digested in a shaking water bath for 60 min at 37°C. The supernatant was neutralized by the addition of phenol red-free DMEM/F12 medium supplemented with 10% FBS before the cells were passed through a 40 m nylon filter (BD Biosciences, Bedford, UK). The undigested tissue fragments were left on the filter, and the stromal cell-containing eluate was transferred into a 50 ml tube. The cells were then pelleted by centrifuging them at 1200 g for 3 min at room temperature. Following that, the cell pellets were washed, resuspended, and seeded in phenol red-free DMEM/F12 media with antibiotics (100 U/ml penicillin and 100 μg/ml streptomycin, Life Technologies, Inc.), 10% FBS, 30 nM 17β estradiol (E2; Sigma Aldrich), and 1 μM progesterone (P4; Sigma Aldrich). All decidual stromal cell cultures were afterwards maintained at 37°C in a humid incubator with 5% CO2, unless otherwise stated, in this culture medium. The purity of the HDSCs was determined by immunofluorescent staining for vimentin and cytokeratin-7 as described previously (Zhu et al., 2007 (link)). HDSCs were cultivated at a density of 5 × 105 cells per plate in 60-mm tissue culture dishes for the time- and concentration-dependent studies, and BMP2 was added in the same manner as HESCs.
Luo J., Wang Y., Chang H.M., Zhu H., Yang J, & Leung P.C. (2023). ID3 mediates BMP2-induced downregulation of ICAM1 expression in human endometiral stromal cells and decidual cells. Frontiers in Cell and Developmental Biology, 11, 1090593.
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Publication 2023
Antibiotics Bath BMP2 protein, human Cells Cold Temperature collagenase 1 Culture Media Decidua Deoxyribonucleases Enzymes Estradiol Human Embryonic Stem Cells Hyaluronidase Hyperostosis, Diffuse Idiopathic Skeletal Immunofluorescence Keratin-7 Nylons Pellets, Drug Penicillins Phosphates Progesterone Saline Solution Streptomycin Stromal Cells Tissues Vimentin
5
Dissecting Notch Signaling Pathways
Cell lysates of ALDH−, ALDH+, and CD44+/CD24− cells following treatment with vehicle and treatment (ASR490, DAPT, MG132, CHX, or CQ) for prescribed doses and time points, were prepared with RIPA buffer (Thermo Scientific, Rockford, IL, United States) per the manufacturer’s protocol. Western blotting was performed using specific antibodies against Notch1 (CST, #3608), HES1 (Sigma, #SAB2108472), Hey1 (Proteintech, #19929-1-AP), NFκB p65 (CST, #8242), Bcl-2 (CST, #15071), Bcl-xL (CST, #2764), Vimentin (CST, #46173), Slug (CST, #9585), E-Cadherin (CST, #3195), β-catenin (CST, #8480), Ubiquitin (CST, #3933), Cleaved-PARP (CST, #5625), Cleaved-caspase-9 (CST, #20750), BAX (CST, #41162), Notch2 (CST, #D76A6), Lamp1 (CST, #9091), and LC3B (Proteintech, #14600-1-AP). β-Actin (CST, #4970) was used as the loading control. Protein bands were visualized using the Bio-Rad ChemiDocTM imaging system. For IP experiments, protein samples were immunoprecipitated with Notch1 antibody as per the protocol described elsewhere (Chandrasekaran et al., 2020 (link)), and Western blots were performed with ubiquitin antibody.
Saran U., Chandrasekaran B., Tyagi A., Shukla V., Singh A., Sharma A.K, & Damodaran C. (2023). A small molecule inhibitor of Notch1 modulates stemness and suppresses breast cancer cell growth. Frontiers in Pharmacology, 14, 1150774.
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Publication 2023
1,2-dilinolenoyl-3-(4-aminobutyryl)propane-1,2,3-triol Actins Antibodies BCL2 protein, human beta-Catenin Buffers Caspase 9 CD44 protein, human CDH1 protein, human Cells Immunoglobulins lysosomal-associated membrane protein 1, human MG 132 NOTCH2 protein, human Proteins Radioimmunoprecipitation Assay Slugs Transcription Factor RelA Ubiquitin Vimentin Western Blot

Top products related to «Vimentin»

1
Vimentin by Cell Signaling Technology
Sourced in United States, United Kingdom, China, France, Denmark, Macao
Vimentin is a protein commonly used as a marker for mesenchymal cells and their derivatives. It is a type III intermediate filament that is important for maintaining cell structure and integrity.
2
E cadherin by Cell Signaling Technology
Sourced in United States, United Kingdom, China, Germany, Canada, Japan, France, Macao, Morocco
E-cadherin is a cell-cell adhesion molecule that plays a crucial role in maintaining the structural and functional integrity of epithelial tissues. It is a transmembrane protein that mediates homophilic interactions between neighboring cells, contributing to the formation and stability of adherens junctions.
3
Vimentin by Abcam
Sourced in United States, United Kingdom, China, Canada, Germany, Hong Kong
Vimentin is a type III intermediate filament (IF) protein that is expressed in mesenchymal cells. It plays a role in maintaining cell integrity and is involved in several cellular processes, including cell migration, signal transduction, and organelle organization.
4
Pvdf membrane by Merck Group
Sourced in United States, Germany, China, United Kingdom, Morocco, Ireland, France, Italy, Japan, Canada, Spain, Switzerland, New Zealand, India, Hong Kong, Sao Tome and Principe, Sweden, Netherlands, Australia, Belgium, Austria
PVDF membranes are a type of laboratory equipment used for a variety of applications. They are made from polyvinylidene fluoride (PVDF), a durable and chemically resistant material. PVDF membranes are known for their high mechanical strength, thermal stability, and resistance to a wide range of chemicals. They are commonly used in various filtration, separation, and analysis processes in scientific and research settings.
5
N cadherin by Cell Signaling Technology
Sourced in United States, China, United Kingdom, Italy, Morocco
N-cadherin is a cell adhesion molecule that plays a crucial role in the formation and maintenance of cell-cell junctions. It is a transmembrane protein that mediates calcium-dependent homophilic interactions between neighboring cells, contributing to the structural integrity and organization of tissues.
6
E cadherin by Abcam
Sourced in United States, United Kingdom, China, Germany, Hong Kong, Japan, Canada, France
E-cadherin is a cell-cell adhesion molecule that plays a crucial role in maintaining the integrity and organization of epithelial tissues. It is a transmembrane glycoprotein that mediates calcium-dependent cell-cell adhesion, contributing to the formation and stabilization of cell-cell junctions.
7
Anti vimentin by Cell Signaling Technology
Sourced in United States, United Kingdom, China, Japan, Germany
Anti-vimentin is a lab equipment product that targets the vimentin protein. Vimentin is a type III intermediate filament protein that is widely expressed in various cell types. Anti-vimentin is a tool used in research applications to detect and analyze the expression and localization of vimentin in biological samples.
8
Ab92547 by Abcam
Sourced in United States, United Kingdom, China
Ab92547 is a laboratory equipment product offered by Abcam. It is designed to perform a specific function in a laboratory setting. The core function of this product is to provide a tool for researchers to use in their experiments, but without further details about its exact capabilities or intended applications.
9
Vimentin by Santa Cruz Biotechnology
Sourced in United States, United Kingdom, China, Germany, Canada
Vimentin is a cytoskeletal protein that is widely expressed in various cell types. It is a type III intermediate filament protein that plays a role in maintaining cell structure, cell signaling, and cell migration. Vimentin is commonly used as a marker for mesenchymal cells and is often used in research applications to study cell biology and developmental processes.
10
N cadherin by Abcam
Sourced in United States, United Kingdom, China, Canada, Hong Kong, Denmark
N-cadherin is a cell adhesion molecule that plays a role in calcium-dependent cell-cell adhesion. It is involved in the formation and maintenance of tissues and organs.

More about "Vimentin"

Vimentin is a type III intermediate filament protein that is widely expressed in various cell types, particularly in cells of mesenchymal origin.
It is also known as VMT or VIM.
This crucial structural protein plays a key role in maintaining the integrity and stability of cells.
Vimentin's expression is often used as a marker for epithelial-to-mesenchymal transition (EMT) and cancer metastasis, as it is involved in cell migration, adhesion, and signaling processes.
Researchers studying vimentin can leverage PubCompare.ai's AI-driven protocol comparison tool to optimize their experiments, locate the best protocols from literature, preprints, and patents, and identify the most reproducible solutions for their vimentin research.
This powerful tool can enhance scientific reproducibility and drive breakthroughs in the understanding of vimentin's function and its role in disease.
Vimentin is closely related to other cell adhesion molecules, such as E-cadherin and N-cadherin, which are also important markers for EMT and cancer progression.
Antibodies like Anti-vimentin (Ab92547) are commonly used to detect and quantify vimentin expression in various experimental and clinical applications.
By utilizing the insights gained from the MeSH term description and the metadescription, researchers can enhance their vimentin studies and make informed decisions to advance their scientific understanding and discoveries.