Mouse anti vimentin

Manufactured by BD

Sourced in United States

Mouse anti-vimentin is a primary antibody used for the detection and analysis of vimentin, an intermediate filament protein expressed in various cell types. This antibody is a valuable tool for researchers studying cellular structure, differentiation, and cytoskeletal organization.

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Lab products found in correlation

8 protocols using mouse anti vimentin

Investigating Cytokine and Signaling Pathways in EMT

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Human recombinant IL-6 and IL-6 neutralizing antibody were purchased from R&D Systems Inc. (Minneapolis, MN, USA). STAT3 inhibitor Stattic was purchased from Sigma-Aldrich Inc. (St Louis, MO, USA), JAK2 inhibitor AG490 was purchased from Abcam (Cambridge, MA, USA).
Antibodies used for western blotting were mouse anti-E-cadherin (Invitrogen, Carlsbad, CA, USA), mouse anti-vimentin (BD Bioscience, San Jose, CA, USA), rabbit anti-phospho-JAK2 (Cell Signaling Technology, Beverly, MA, USA), rabbit anti-STAT3 (Cell Signaling Technology), rabbit anti-phospho-STAT3 (Cell Signaling Technology), mouse anti-α-SMA (Abcam), rabbit anti-MMP2 (Cell Signaling Technology), mouse anti-VEGF (Cell Signaling Technology), rabbit anti-TWIST (Cell Signaling Technology), mouse anti-β-actin (Sigma-Aldrich). The secondary antibodies coupled to HRP were purchased from ZSGB-BIO (Beijing, China)

Wang L., Cao L., Wang H., Liu B., Zhang Q., Meng Z., Wu X., Zhou Q, & Xu K. (2017). Cancer-associated fibroblasts enhance metastatic potential of lung cancer cells through IL-6/STAT3 signaling pathway. Oncotarget, 8(44), 76116-76128.

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Comprehensive Antibody Panel for Western Blot Analysis

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The following primary antibodies used for Western Blot analyses were from Cell Signaling technology, at a dilution of (1:1000): rabbit anti pERK1/2, rabbit anti ERK1/2, rabbit anti Keratin 5. Rabbit anti Kindlin-1 (1:1000), mouse anti Kindlin-2 (1:1000), and rabbit anti Kindlin-3 (1:1000) were obtained from ProCsi, and rabbit anti-pSMAD3 (1:1000) and rabbit anti-SMAD3 (1:1000) were obtained from Abcam; mouse anti-Vimentin (1:2000) was obtained from BD Pharmingen, and mouse monoclonal anti β-actin was obtained from Sigma-Aldrich (1:5000). Secondary antibodies—goat horseradish-peroxidase-conjugated anti-mouse IgG and goat horseradish-peroxidase-conjugated anti-rabbit IgG (1:2000)—were ordered from BioRad. The antibodies were dissolved to a working concentration either in 5% BSA (primary antibodies) or 5% Non-Fat Dry Milk (secondary antibodies).

Wang W., Rana P.S., Alkrekshi A., Bialkowska K., Markovic V., Schiemann W.P., Plow E.F., Pluskota E, & Sossey-Alaoui K. (2022). Targeted Deletion of Kindlin-2 in Mouse Mammary Glands Inhibits Tumor Growth, Invasion, and Metastasis Downstream of a TGF-β/EGF Oncogenic Signaling Pathway. Cancers, 14(3), 639.

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Immunofluorescence Analysis of Epithelial-Mesenchymal Transition in HIOs

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HIOs were fixed in 4% paraformaldehyde (Electron Microscopy Sciences, Hatfield, PA, USA), transferred to 30% sucrose overnight at 4 °C, embedded in Tissue-Tek O.C.T Compound (VWR, Radnor, PA, USA), and cut into 10-μm sections. Sections were blocked in 10% normal donkey serum (Jackson ImmunoResearch, West Grove, PA, USA) with 0.5% Triton X-100 and incubated with the following primary antibodies: goat anti-mouse/human E-cadherin (AF648; R&D Systems) and mouse anti-vimentin (#550513; BD Biosciences, San Jose, CA, USA) for either 4 hours at room temperature or overnight at 4 °C. Sections were then rinsed and incubated in species-specific AF488 or AF647-conjugated secondary antibodies (Life Technologies, Carlsbad, CA, USA) followed by DAPI (0.5 μg/mL; Life Technologies, Carlsbad, CA, USA) to counterstain nuclei and were imaged using a Leica DM6000 B microscope (Leica, Wetzlar, Germany).

Estrada H.Q., Patel S., Rabizadeh S., Casero D., Targan S.R, & Barrett R.J. (2021). Development of a Personalized Intestinal Fibrosis Model Using Human Intestinal Organoids Derived From Induced Pluripotent Stem Cells. Inflammatory Bowel Diseases, 28(5), 667-679.

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Western Blotting of EMT Markers

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Western blotting was performed as described previously using whole cell lysates [14 (link)]. Cells were harvested to prepare cell lysates two weeks after initiating of mutant KRAS^V12 induction. Primary antibodies used were mouse anti-E-cadherin (Cat#610181, BD Biosciences), mouse anti-Vimentin Cat#550513, BD Biosciences), mouse anti-p53 (Cat#sc-126, Santa Cruz, USA), mouse anti-p21 Waf/Cip/CDKN1A (Cat#sc-6246, Santa Cruz), mouse anti-KRAS (Cat#sc-30, Santa Cruz), rabbit anti-AKT (pan) (Cat#4691, Cell Signaling Technology), rabbit anti-phospho-AKT (ser 473) (Cat#4060, Cell Signaling Technology), rabbit anti-p44/42MAPK(Erk1/2) (Cat#9102, Cell Signaling Technology), rabbit anti-phospho-p44/42MAPK(Erk1/2) (Cat#4370, Cell Signaling Technology), mouse anti-Actin (Cat#A2228, Sigma-Aldrich), mouse anti-Vinculin (Cat#SC-73614, Santa Cruz), rabbit anti-α-tubulin (Cat# PM054-7, MBL Life Science, USA), and rabbit anti-phospho-p53 (Ser 15) (Cat#9284, Cell Signaling Technology) antibodies. Actin, Vinculin, or α-tubulin protein levels were used as a control for the adequacy of equal protein loading. Anti-rabbit or anti-mouse (GE Healthcare, Buckinghamshire, England) antibodies were used at 1:2000 dilution as secondary antibodies.

Bisgaard H, & Møller H. (1999). Changes in risk of hospital readmission among asthmatic children in Denmark, 1978-93. BMJ : British Medical Journal, 319(7204), 229-230.

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Immunohistochemical Analysis of EMT Markers

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Primary antibodies used were as follows: Rabbit anti-YAP1 (#14074, Cell signaling Technology, Whitby, ON, Canada); Mouse anti-vimentin (#550513), Mouse anti-E-Cadherin (#610181) and Mouse anti-Ki67 (#556003) were from BD BIOSCIENCES (Franklin Lakes, NJ, USA); Rabbit anti-ZEB1 (#ABD53), Rabbit anti-total Fibronectin (#F3648), Mouse anti-laminin-V (#MAB19562), and Mouse pan-anti-Cytokeratin AE1/AE3 (#MAB3412) were from MilliporeSigma (Billerica, MA, USA); Rabbit anti-vimentin (#ab45939), Rabbit anti-MMP9 (#ab76003) were from Abcam (San Francisco, CA, USA). Secondary antibodies used were as follows: Goat anti-Mouse Alexa Fluor 488 (#A11001), Goat anti-Rabbit Alexa-Fluor 488 (#A11029), Goat anti-Rabbit Alexa-Fluor 594 (#A11037), and Goat anti-Mouse Alexa-Fluor 594 (#A11032) were from Thermo Fisher Scientific. All other chemicals were from MilliporeSigma unless specified.

Millet M., Bollmann E., Ringuette Goulet C., Bernard G., Chabaud S., Huot M.É., Pouliot F., Bolduc S, & Bordeleau F. (2022). Cancer-Associated Fibroblasts in a 3D Engineered Tissue Model Induce Tumor-like Matrix Stiffening and EMT Transition. Cancers, 14(15), 3810.

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Molecular Cloning and Antibody Validation

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Human MDA-9/Syntenin cDNA were obtained from H1299 by RT-PCR. Its full length or deletion constructs were sub-cloned into pACT2, pcDNA3.1-HA, pCMV-tag2 (Clontech, CA, USA), pEGFP (Invitrogen), and pLKO.1-AS2-neo vectors for the production of lentivirus or pET28a vectors for bacterial expression by standard molecular cloning procedure. Flag-tagged Slug was as described previously [10 (link)]. Full length or deletion constructs of Slug were sub-cloned into pAS2–1, pCI-neo, pcDNA3.1-HA, pDsRED, and AS2-neo vectors. pcDNA3-HDAC1-Flag was kindly provided by Dr. Wen-Ming Yang (Institute of Molecular Biology, National Chung Hsing University, Taichung, Taiwan).
The primary antibodies used for immunoblot analysis were anti-Syntenin (mouse monoclonal, S-31 or rabbit polyclonal, H-48, Santa Cruz Biotechnology, CA, USA and rabbit monoclonal, Abcam, MA, USA), goat anti-Slug (Santa Cruz Biotechnology), goat anti-HDAC1 (Santa Cruz Biotechnology) and mouse anti-β-actin (Santa Cruz Biotechnology), mouse anti-Flag (Sigma-Aldrich, MO, USA), mouse anti-HA (Covance, Berkeley, California, USA), mouse anti-E-cadherin (BD Biosciences, Inc., CA, USA), mouse anti-vimentin (BD Biosciences), mouse anti-N-cadherin (BD Biosciences), and mouse anti-GFP (BD Biosciences).

Wang L.K., Pan S.H., Chang Y.L., Hung P.F., Kao S.H., Wang W.L., Lin C.W., Yang S.C., Liang C.H., Wu C.T., Hsiao T.H., Hong T.M, & Yang P.C. (2015). MDA-9/Syntenin-Slug transcriptional complex promote epithelial-mesenchymal transition and invasion/metastasis in lung adenocarcinoma. Oncotarget, 7(1), 386-401.

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Identifying Inflammatory Markers in Arthritis

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Antigens were retrieved by incubating joint sections at 60 °C overnight with sodium citrate buffer (10 mM sodium citrate, 0.05% Tween 20, pH 6.0). The sections were blocked with 2% bovine serum albumin in phosphate-buffered saline (PBS), and then incubated with primary antibodies, including rabbit anti-BATF (Brookwood Biomedical), rabbit anti-RANKL (receptor activator of NF-κB ligand) (Abcam), goat anti-IL-6 (R&D Systems), rabbit anti-TNF-α (tumor necrosis factor alpha) (Novus Biologicals), and rabbit anti-Ki67 (Abcam). The Dako REAL Envision Detection system was used for chromogenic color development. BATF-expressing cells in synovial tissues were identified by double immunofluorescence labeling of vimentin for FLS, CD11b for macrophages, CD4 for T cells, and B220 for B cells. The following primary antibodies were used: mouse anti-CD4, mouse anti-B220, rat anti-CD11b (Abcam), rabbit anti-BATF (ThermoFisher Scientific), and mouse anti-vimentin (BD Pharmingen). Blood vessels in synovial tissues were detected with mouse anti-CD31 (Dianova). TRAP activity was determined in joint sections as previously described [20 (link), 22 (link)], and the numbers of TRAP-positive osteoclasts were counted in regions containing pannus-cartilage and pannus-bone interfaces.

Park S.H., Rhee J., Kim S.K., Kang J.A., Kwak J.S., Son Y.O., Choi W.S., Park S.G, & Chun J.S. (2018). BATF regulates collagen-induced arthritis by regulating T helper cell differentiation. Arthritis Research & Therapy, 20, 161.

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Comprehensive Protein Extraction and Analysis

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Total proteins were extracted as previously described.14 (link) Tissues and cells were lysed in RIPA buffer (Beyotime, China), and protein concentrations were measured using the bicinchoninic acid protein assay kit (Pierce, Rockford, IL, USA). Equal protein extracts were run on SDS-PAGE and subsequently transferred to a polyvinylidene fluoride membrane (Millipore, Billerica, MA, USA). After the membrane was blocked for 1 hour using 5% skim milk, it was incubated with a primary antibody overnight at 4°C. Finally, the membrane was incubated with their respective horseradish peroxidase-conjugated secondary antibodies (Santa Cruz Biotechnology Inc., Santa Cruz, CA, USA) for 2 hours. The sources of the antibodies and their concentrations are as follows: rabbit anti-PKM2 (1:1000, CST), rabbit anti-c-Myc (1:1000, CST), mouse anti-E-cadherin (1:1000, BD), mouse anti-vimentin (1:1000, BD), mouse anti-β-catenin (1:1000, Santa Cruz Biotechnology Inc.), rabbit anti-slug (1:1000, CST), rabbit anti-snail (1:1000, CST), rabbit anti-cycline D1 (1:1000, CST), and rabbit anti-glyceraldehyde-3-phosphate dehydrogenase (1:1000, CST). The protein bands of interest were visualized using enhanced chemiluminescence reagents (Millipore, Burlington, MA, USA).

Lin Y., Meng F., Lu Z., Chen K., Tao Y., Ouyang Y, & Cao X. (2018). Knockdown of PKM2 suppresses tumor progression in human cervical cancer by modulating epithelial–mesenchymal transition via Wnt/β-catenin signaling. Cancer Management and Research, 10, 4191-4202.

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