Anti vinculin hvin 1

Manufactured by Merck Group

Sourced in Spain, United Kingdom, Japan

Anti-Vinculin hVIN-1 is a laboratory reagent used to detect and quantify the presence of the vinculin protein in biological samples. Vinculin is a key component of cell-cell and cell-matrix adhesion complexes. Anti-Vinculin hVIN-1 is a monoclonal antibody that specifically binds to the vinculin protein, allowing researchers to study its expression and localization in various cell types and tissues.

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Lab products found in correlation

Rabbit anti zo 1, by Thermo Fisher Scientific (2 mentions) Alexa fluor 568, by Thermo Fisher Scientific (2 mentions) Ab73895, by Abcam (1 mentions) Alexa fluor 488, by Thermo Fisher Scientific (1 mentions) Anti hif 2α ab199, by Abcam (1 mentions) Anti α tubulin t6199, by Merck Group (1 mentions) Anti β actin, by Cell Signaling Technology (1 mentions) Alexa fluor 568 phalloidin, by Thermo Fisher Scientific (1 mentions) Nupage bis tris gel, by Thermo Fisher Scientific (1 mentions) Odyssey clx imaging system, by LI COR (1 mentions) Anti actin, by Merck Group (1 mentions) Anti α tubulin b 5 1 2, by Merck Group (1 mentions) Imagequant las 4000, by GE Healthcare (1 mentions) Amersham ecl prime western blotting detection reagent, by GE Healthcare (1 mentions) Anti flag m2, by Merck Group (1 mentions) Donkey anti goat hrp conjugated igg, by R&D Systems (1 mentions) Triton x 100, by Merck Group (1 mentions) Complete protease inhibitor cocktail, by Merck Group (1 mentions) Dc protein assay, by Bio-Rad (1 mentions) Tween 20, by Merck Group (1 mentions)

Close spelling variants of this product

Mouse monoclonal anti-Vinculin (hVIN-1) Anti-vinculin (clone hVIN-1, Mouse anti-vinculin (clone hVIN-1, Mouse anti-vinculin hVin-1 Vinculin (hVIN-1; HVIN-1 Anti-vinculin Vinculin

6 protocols using anti vinculin hvin 1

Measuring Angiogenic Factors in Samples

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The following reagents were employed: mouse anti-TSP1 clone A6.1 (Pierce, Alcobendas, Spain), TSP1 in human samples was detected with monoclonal anti-TSP1 ab1823 (Abcam, Cambridge, UK), HIF-2α was detected with anti-HIF-2α ab199 (mice) or ab73895 (human; Abcam), and HIF-1α was detected with polyclonal anti-HIF-1α C-term (Cayman Chemical Company, Ann Arbor, MI, USA), or monoclonal anti-HIF-1-a (610958, BD Biosciences, human samples) anti-Vinculin hVIN-1 (Sigma-Aldrich, Tres Cantos, Spain), anti-α-Tubulin T6199 (Sigma-Aldrich), anti-β-Actin (Cell Signaling Technology, Danvers, MA, USA), and rabbit anti-ZO-1 (Thermo Fisher Scientific, Alcobendas, Spain). Secondary antibodies were anti-IgG + IgM of mouse and rabbit conjugated with Peroxidase (Pierce), as well as goat anti-rabbit and goat anti-mouse antibodies conjugated with Alexa Fluor 488 (Invitrogen, Alcobendas, Spain). Alexa Fluor 568 phalloidin (Life Technologies, Alcobendas, Spain). TSP1 from human platelets was obtained from (Athens Research and Technology, Athens, GA, USA).

Labrousse-Arias D., Castillo-González R., Rogers N.M., Torres-Capelli M., Barreira B., Aragonés J., Cogolludo Á., Isenberg J.S, & Calzada M.J. (2015). HIF-2α-mediated induction of pulmonary thrombospondin-1 contributes to hypoxia-driven vascular remodelling and vasoconstriction. Cardiovascular Research, 109(1), 115-130.

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Immunofluorescence Staining of Muscle Proteins

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Anti-paxillin (349, 1:100) was from BD Biosciences. Anti-vinculin (hVin1, 1:5000) was from Sigma. Anti-actinin2 (ab9465, 1:500) was from Abcam. Anti-actinin2 c-terminal (70R-1068, 1:200) was from Fitzgerald. Anti-NMM IIA (PRB-440P, 1:1000) and NMM IIB (PRB-445P, 1:1000) were from Biolegend. Anti-NMM IIB was directly conjugated with Alexa Fluor 568 (ThermoFisher), allowing the simultaneous immunofluorescent staining of NMM IIA and NMM IIB (Figure S2b). Anti-MHC (MF-20, 1:1000) was from DSHB. Anti-MHC-α (22281–1-AP, 1:5000) and Anti-MHC-β (22280–1-AP, 1:5000) were from Protein Tech Group (Chicago, IL). Blebbistatin± (racemic) was from CalBioChem.

Chopra A., Kutys M.L., Zhang K., Polacheck W.J., Sheng C.C., Luu R.J., Eyckmans J., Hinson J.T., Seidman J.G., Seidman C.E, & Chen C.S. (2018). Force generation via β-cardiac myosin, titin, and α-actinin drives cardiac sarcomere assembly from cell-matrix adhesions. Developmental cell, 44(1), 87-96.e5.

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Immunoblotting Analysis of Cell Extracts

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Whole-cell extracts were prepared by lysis using 50 mM Tris-HCl (pH 8), 280 mM NaCl, 0.5% NP40, 0.2 mM EGTA, 1 mM DTT, and 10% glycerol, supplemented with Roche Complete protease inhibitor cocktail. Protein samples were resolved on 4%–12% NuPAGE Bis-Tris gels (Thermo Fisher Scientific) and transferred to nitrocellulose or PVDF membranes. Subsequent immunoblotting was performed using the following antibodies: anti-p48 Primase (8G10; 1:1000; Cell Signaling 4725), anti-Vinculin (hVIN-1; 1:2000; Sigma-Aldrich, V9264), anti-α-Tubulin (B-5-1-2; 1:10,000; Sigma-Aldrich, T6074), anti-GFP (Living Colors JL-8; 1:4000; Clontech), anti-FLAG (M2; 1:2000; Sigma-Aldrich F1804), or anti-Actin (1:4000; Sigma-Aldrich A2066).
Finally, detection was performed using Amersham ECL Prime Western blotting detection reagent on the ImageQuantLAS4000 (GE Healthcare Life Sciences), or the Odyssey CLx imaging system (LI-COR Biosciences). Quantifications were performed using ImageQuant TL 7.0 and Image Studio Lite 5.2, respectively.

Parry D.A., Tamayo-Orrego L., Carroll P., Marsh J.A., Greene P., Murina O., Uggenti C., Leitch A., Káposzta R., Merő G., Nagy A., Orlik B., Kovács-Pászthy B., Quigley A.J., Riszter M., Rankin J., Reijns M.A., Szakszon K, & Jackson A.P. (2020). PRIM1 deficiency causes a distinctive primordial dwarfism syndrome. Genes & Development, 34(21-22), 1520-1533.

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Quantifying Lung Fungal Infection and C3 Levels

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Lungs were removed 16 h after infection and homogenized in 1 ml PBS, pH 7.4, containing 0.01% (vol/vol) Tween-20^® (Merck-Millipore) and protease inhibitors. Samples were serially diluted 1:10 in PBS and plated on Sabouraud dextrose agar for blinded CFU counting. For lysate preparation, lungs were collected at 4 h and homogenized in 50 mM Tris-HCl, pH 7.5, containing 2 mM EGTA, 1 mM PMSF, 1% Triton X-100 (all from Sigma-Aldrich/Merck), and complete protease inhibitor cocktail. Total proteins were measured by DC Protein Assay, according to manufacturer’s instructions (Bio-Rad Laboratories). Western blot analysis for C3 was performed after loading 10 µg of lung protein extracts on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The goat polyclonal anti-C3 (diluted 1:3000; Merck-Millipore, Cat. No. 204869) and HRP-conjugated donkey anti-goat IgG (diluted 1:5000; R&D Systems, Cat. No. HAF-109) were used. The monoclonal anti-vinculin (#hVIN-1; used at 0.5 µg/ml; Sigma-Aldrich/Merck, Cat. No. V9264) was used as loading control. C3d bands were quantified by Fiji-ImageJ (NIH, Bethesda USA; version 2.1.0/1.53.c) as a ratio of mean gray intensity values of each protein relative to vinculin bands.

Doni A., Parente R., Laface I., Magrini E., Cunha C., Colombo F.S., Lacerda J.F., Campos A J.r., Mapelli S.N., Petroni F., Porte R., Schorn T., Inforzato A., Mercier T., Lagrou K., Maertens J., Lambris J.D., Bottazzi B., Garlanda C., Botto M., Carvalho A, & Mantovani A. (2021). Serum amyloid P component is an essential element of resistance against Aspergillus fumigatus. Nature Communications, 12, 3739.

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Western Blot Analysis of MET, JAK, and STAT Signaling

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Sub-confluent cells were lysed in Laemmli buffer (LB) and 45 µg of total proteins were subjected to SDS-PAGE and western blotting following standard methods. Protein detection was performed by using the following primary antibodies, diluted as indicated: anti-human MET (3D4, 1:3000, Invitrogen Corp., Camarillo, CA), anti-pMET Tyr^1234/1235 (D26, 1:1000), anti-JAK1 (6G4, 1:1000), anti-pJAK1 Tyr^1022/1023 (1:1000), anti-JAK2 (D2E12, 1:1000), anti-pJAK2 Tyr^1007/1008 (1:1000) anti-STAT1 (1:1000), anti-pSTAT1 Tyr⁷⁰¹ (58D6, 1:1000), anti-PD-L1 (E1L3N, 1:1000), anti-GAPDH (D4C6R, 1:1000) (all from Cell Signaling Technology, Beverly, MA), anti-IFNGR1 (EPR7866, 1:1000, Abcam, Cambridge, UK) and anti-Vinculin (hVIN-1, 1:1000, Sigma Life Sciences). Secondary HRP-conjugated goat anti-mouse IgG (1:20,000) or anti-rabbit IgG (1:20,000) (from Jackson ImmunoResearch, Cambridge, UK) and ECL System (Promega, Madison, WI) were used for protein detection.

Martin V., Chiriaco C., Modica C., Acquadro A., Cortese M., Galimi F., Perera T., Gammaitoni L., Aglietta M., Comoglio P.M., Vigna E, & Sangiolo D. (2019). Met inhibition revokes IFNγ-induction of PD-1 ligands in MET-amplified tumours. British Journal of Cancer, 120(5), 527-536.

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Western Blot Analysis of EMT Markers

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Treated cells were lysed in NuPAGE LDS Sample Buffer (Thermo Fisher Scientific). Whole cell lysates were subjected to SDS-PAGE (4-15% Mini-Protean TGX Precast Gels; BIO-RAD, Hercules, CA, USA) followed by blotting with specific antibodies, and detection using the Supersignal West Pico Chemiluminescent Substrate (Thermo Fisher Scientific). The primary antibodies used were anti-E-cadherin (24E10; 1:1000; Cell Signaling), anti-TTF-1 (EPR8190; 1:1000; Abcam Japan, Tokyo, Japan), anti-phospho-SMAD2 (S465/467) (D27F4; 1:1000; Cell Signaling), anti-vimentin (D21H3; 1:1000; Cell Signaling), and anti-vinculin (hVIN-1; 1:5000; Sigma-Aldrich). To evaluate the relative expression levels of E-cadherin, the band intensities were measured on X-ray film using Image J software (National Institutes of Health, Bethesda, MD, USA).

Yamaguchi M., Hirai S., Tanaka Y., Sumi T., Miyajima M., Mishina T., Yamada G., Otsuka M., Hasegawa T., Kojima T., Niki T., Watanabe A., Takahashi H, & Sakuma Y. (2017). Fibroblastic foci, covered with alveolar epithelia exhibiting epithelial-mesenchymal transition, destroy alveolar septa by disrupting blood flow in idiopathic pulmonary fibrosis. Laboratory investigation; a journal of technical methods and pathology, 97(3).

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