Anti caveolin 1

Manufactured by BD

Sourced in United States

Anti-caveolin-1 is a laboratory reagent used to detect and quantify the presence of caveolin-1 protein in biological samples. Caveolin-1 is a structural component of caveolae, which are small invaginations of the cell membrane involved in various cellular processes. The anti-caveolin-1 reagent can be used in techniques such as Western blotting, immunohistochemistry, and immunocytochemistry to analyze the expression and localization of caveolin-1 in different cell types and tissues.

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Lab products found in correlation

Anti flotillin 1, by BD (3 mentions) Anti actin, by Merck Group (2 mentions) Anti fak, by Santa Cruz Biotechnology (2 mentions) Bca protein assay, by Thermo Fisher Scientific (2 mentions) Alexa 647, by Thermo Fisher Scientific (1 mentions) Anti paxillin, by Abcam (1 mentions) Alexa fluor 647, by Thermo Fisher Scientific (1 mentions) Saponin, by Merck Group (1 mentions) Paraformaldehyde (pfa), by Merck Group (1 mentions) Folch fraction 1, by Merck Group (1 mentions) Rpmi medium, by Thermo Fisher Scientific (1 mentions) Anti gfp, by Roche (1 mentions) Chemiluminescent substrate, by PerkinElmer (1 mentions) Horseradish peroxidase, by Merck Group (1 mentions) Anti transferrin receptor, by Zymo Research (1 mentions) Las 4000 image analyzer, by Fujifilm (1 mentions) Anti rac1, by BD (1 mentions) Anti gfp, by Nacalai Tesque (1 mentions) Horseradish peroxidase conjugated igg, by Cytiva (1 mentions) Anti ha, by Roche (1 mentions)

Close spelling variants of this product

Mouse anti-Caveolin-1 (6 citations) Rabbit anti-caveolin-1 antibody (2 citations) Anti-caveolin-1 antibody (2 citations) Mouse anti-Caveolin-1 antibodies (2 citations) Rabbit anti-caveolin 1 (8 citations) Caveolin-1 (18 citations) Anti-Caveolin (4 citations)

15 protocols using anti caveolin 1

Immunofluorescence Staining of Fixed Cells

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For fixed-cell experiments, after the treatments above cells were washed twice with HBSS and incubated with 4% paraformaldehyde (Sigma) in PBS for 20 min at room temperature followed by two washes with PBS.
For immunofluorescence experiments, fixed-cell samples were permeabilized with 0.1% saponin (Sigma) in PBS for 5 min. The antibodies used for staining were anti-clathrin heavy chain (provided by D. Billadeau and T. Gomez; 1:1000), anti-caveolin-1 (BD Transduction; 1:500), and anti-paxillin (Abcam; 1:1000) antibodies. Secondary antibodies conjugated with Alexa Fluor 647 (Invitrogen) were used. For F-actin staining, phalloidin conjugated with Alexa 647 (Invitrogen) was used.

Kim S., Kalappurakkal J.M., Mayor S, & Rosen M.K. (2019). Phosphorylation of nephrin induces phase separated domains that move through actomyosin contraction. Molecular Biology of the Cell, 30(24), 2996-3012.

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Culturing and Immunostaining of PC3 and MCF7 Cells

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PC3 cells were maintained in RPMI medium (Gibco® Life technologies) supplemented with 10% foetal bovine serum (FBS) and Penicillin/Streptomycin. Cell lines were sourced from ATCC and tested fortnightly for mycoplasma contamination. For all experiments, 2 × 105 PC3 or MCF7 cells were plated in either 6 well culture dishes (Nunc™, Cat. No. 140675, Culture area—9.6 cm²) or glass bottom 35 mm dishes (ibidi, No. 1.5 glass coverslip bottom Cat No. 81218) or 35 mm tissue culture dishes (TPP^® 93040, culture area—9.2 cm²). Antibodies used were as follows, rabbit polyclonal anti-Caveolin1 (BD Transduction Laboratories, Cat. No. 610060, Dilution 1:1000), mouse monoclonal anti-GFP (Roche Diagnostics Cat. No. 11814460001, Dilution 1:1000), Donkey anti-Rabbit IgG (H + L) Secondary Antibody Alexa Fluor® 555 conjugate (Thremo Fisher Scientific, Cat No. A31572, Dilution 1:400). Mouse monoclonal anti-tubulin (Anti-alpha Tubulin antibody [DM1A] - Abcam (ab7291), Dilution 1:1000). Folch lipids were obtained from Sigma Aldrich Folch I fraction (B1502).

Tillu V.A., Rae J., Gao Y., Ariotti N., Floetenmeyer M., Kovtun O., McMahon K.A., Chaudhary N., Parton R.G, & Collins B.M. (2021). Cavin1 intrinsically disordered domains are essential for fuzzy electrostatic interactions and caveola formation. Nature Communications, 12, 931.

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Antibody Detection for Caveolins and PTRF

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Monoclonal antibodies recognizing PTRF (2F11), caveolin-1 (7C8), have been previously described (Souto et al., 2003 (link); Vinten et al., 2001 (link)). The following antibodies were commercially acquired: anti-caveolin-1 was from BD Transduction Laboratories (San Jose, CA), anti-actin was from Sigma; anti-transferrin receptor was from Zymed Laboratories (South San Francisco, CA). Additional anti-PTRF antibodies were purchased from BD Transduction. Polyclonal rabbit anti-PTRF antibody was also produced against a peptide sequence at the C terminus of the protein (21st Century Biochemicals, Hopkinton, MA). Primary antibodies were detected in Western blots using secondary antibodies conjugated to horseradish peroxidase (Sigma) diluted 1:3000 and chemiluminescent substrate (PerkinElmer Life Sciences, Boston, MA), followed by detection by Fujifilm LAS-4000 Image Analyzer.

Liu L, & Pilch P.F. (2016). PTRF/Cavin-1 promotes efficient ribosomal RNA transcription in response to metabolic challenges. eLife, 5, e17508.

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Antibody Protocols for Cell Analysis

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We used commercial rat and mouse antibodies: anti-GFP (Nacalai), anti-HA (Roche Diagnostics, Cell Signaling), anti-Flotillin-1, anti-Caveolin-1, anti-Rac1, anti-GM130 (BD), horseradish peroxidase-conjugated IgG (Amersham Biosciences), and Alexa 488-, Alexa 555-, and Alexa 594-conjugated IgG (Molecular Probes).

Ageta-Ishihara N., Takemoto-Kimura S., Kondo Y., Okamura M, & Bito H. (2023). Lipidation states orchestrate CLICK-III/CaMKIγ's stepwise association with Golgi and rafts-enriched membranes and specify its functional coupling to STEF-Rac1-dependent neurite extension. Frontiers in Cellular Neuroscience, 17, 1204302.

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Immunoblotting of Cell Signaling Proteins

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Cells were washed with PBS and lysed with n-octyl-β-D-glucoside (ODG) buffer [20 mM Tris-HCl (pH 7.4), 150 mM sodium chloride, 1 mM EDTA, 1 mM sodium orthovanadate, 20 mM sodium fluoride, 1% Nonidet P-40, 5% glycerol, 2% ODG, and a protease inhibitor cocktail], and immunoblotting was carried out as described previously [26] (link). The following primary antibodies were used: anti-Src (Ab-1; Calbiochem), anti-Src pY418 (Invitrogen), anti-phosphotyrosine (4G10; Millipore), anti-cortactin (Sigma), anti-cortactin pY421 (Sigma), anti-FAK (Santa Cruz), anti-FAK pY576 (Cell Signaling), anti-ERK pT202/Y204 (Cell Signaling), anti-ERK (Cell Signaling), anti-GAPDH (Sigma), anti-Flottilin-1 (BD) and anti-Caveolin-1 (BD). Anti-Cbp and anti-Cbp pY314 were prepared as described previously [19] (link). GAPDH was used as a loading control. Horseradish peroxidase (HRP)–conjugated anti-mouse or anti-rabbit IgG (Zymed) was used as the secondary antibody. All blots were visualized and quantitated using a LAS-4000 luminescent image analyzer (GE Healthcare).

Saitou T., Kajiwara K., Oneyama C., Suzuki T, & Okada M. (2014). Roles of Raft-Anchored Adaptor Cbp/PAG1 in Spatial Regulation of c-Src Kinase. PLoS ONE, 9(3), e93470.

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Antibody Sources for Cellular Imaging

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Different anti-OXPHOS antibodies were obtained from Molecular Probes (Carlsbad,
California, USA) and Santa Cruz Biotechnology (Santa Cruz, CA, USA).
Anti-cytochrome c, anti-caveolin-1 and anti-caveolin-3
antibodies were obtained from BD Biosciences (Franklin Lakes, New Jersey, USA).
MitoTracker Red FM dye and Alexa Fluor 488-conjugated anti-mouse IgG were
purchased from Invitrogen (Carlsbad, California, USA). FITC-conjugated
anti-mouse IgG and Rhodamine-conjugated anti-rabbit IgG were obtained from Abcam
(Cambridge, UK). Collagenase type I and bovine serum albumin (BSA) were
purchased from Sigma (St. Louis, Missouri, USA).

Lee H., Kim S.H., Lee J.S., Yang Y.H., Nam J.M., Kim B.W, & Ko Y.G. (2016). Mitochondrial oxidative phosphorylation complexes exist in the sarcolemma of skeletal muscle. BMB Reports, 49(2), 116-121.

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Histological Analysis of Embryonic Lung Development

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Embryos and tissues were fixed in 10% formalin overnight, dehydrated in 100% ethanol, and embedded in paraffin. 8-µm-thick sections were used for hematoxylin-eosin, periodic acid-Schiff (PAS), trichrome, and immunohistochemistry staining. The following primary antibodies were used for immunostaining: anti-LYVE1 (R&D Systems), anti-PROX1 (Abcam), anti-PECAM1 (R&D Systems; clone: 693102), anti–pro-surfactant protein C (pro-SPC; EMD Millipore), anti-Clara cell 10 (CC10; Santa Cruz Biotechnology, Inc.), anti-Podoplanin (Abcam), anti–Caveolin-1 (BD), anti-PDGFRα (Cell Signaling Technology), anti-PDGFRβ (Cell Signaling Technology), anti-SM22α (Abcam), anti-WT1 (Santa Cruz Biotechnology, Inc.), anti-Vimentin (Santa Cruz Biotechnology, Inc.), anti-Desmin (Dako), and anti-NG2 (EMD Millipore). Detailed histology procedures can be found on the University of Pennsylvania Molecular Cardiology Research Center Histology and Gene Expression Core website. Microscopic images were taken on a microscope (Eclipse 80i; Nikon) connected to a camera (DS-Ri1; Nikon). Alveolar wall thickness (averaging 50–100 measurements per embryo) and alveolar area (averaging the total alveolar area in 5–15 vision fields per embryo) were performed in Elements software (Nikon) using a 40× objective.

Jakus Z., Gleghorn J.P., Enis D.R., Sen A., Chia S., Liu X., Rawnsley D.R., Yang Y., Hess P.R., Zou Z., Yang J., Guttentag S.H., Nelson C.M, & Kahn M.L. (2014). Lymphatic function is required prenatally for lung inflation at birth. The Journal of Experimental Medicine, 211(5), 815-826.

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Western Blot Analysis of OCTN2 Protein

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Protein samples were loaded onto 8% polyacrylamide gels. Proteins were transferred onto nitrocellulose membranes (GE HealthCare, Piscataway, NJ, USA). The membranes were blocked with 5% (w/v) nonfat dry milk in PBS supplemented with 0.1% (w/v) Tween 20 and incubated overnight at 4 °C with anti-OCTN2 (NBP2-57222, Novusbio, Littleton, CO, USA), followed by probing with a horseradish peroxidase–conjugated anti-rabbit IgG antibody (G21234, ThermoFisher Scientific). As a control, the sample blots were probed with anti-Na⁺/K⁺ ATPase (ab7671, Abcam, Cambridge, UK), anti-CAVEOLIN-1 (610060, BD biosciences, San Jose, CA, USA) and anti-FLOTILLIN-1 (610821, BD biosciences). Blots were developed with SuperSignal West Femto Maximum Sensitivity Substrate (ThermoFischer Scientific) and Fusion FX7 (Vilber Lourmat, Eberhardzell, Germany).

Zhang L., Gui T., Console L., Scalise M., Indiveri C., Hausler S., Kullak-Ublick G.A., Gai Z, & Visentin M. (2021). Cholesterol stimulates the cellular uptake of L-carnitine by the carnitine/organic cation transporter novel 2 (OCTN2). The Journal of Biological Chemistry, 296, 100204.

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Comprehensive Neuronal Protein Analysis

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All chemicals, unless otherwise stated were purchased from Sigma-Aldrich (St. Louis, MO). The following primary antibodies were used: anti-PSD95 (Santa Cruz Biotechnology, Dallas, TX, catalog #SC-32290), anti-GAPDH (Santa Cruz Biotechnology, Dallas, TX, catalog #SC-25778) anti-flotillin1 (BD Biosciences, San Jose, CA, catalog #610821), anti-caveolin1 (BD Biosciences, San Jose, CA, catalog #610059), anti-α-synuclein (BD Biosciences, San Jose, CA, catalog #610787), anti-synaptophysin (Synaptic Systems, Goettingen, Germany, catalog #101011), anti-Homer (Synaptic Systems, Goettingen, Germany, catalog #160003), anti-synaptotagmin-1 (Synaptic Systems, Goettingen, Germany, catalog #105011) anti-NMDAR2a (Abcam plc, Cambridge, UK, catalog #ab133265), anti-NMDAR2b (Abcam plc, Cambridge, UK, catalog #ab28373), anti-NMDAR2b phospho S1480 (Abcam plc, Cambridge, UK, catalog #ab73014), anti-PKA (Santa Cruz Biotechnology, #sc-390548), and anti-GluA1 (Abcam plc, Cambridge, UK, catalog #ab32436). Syn peptides (amino acids 12–23 and 34–45) were obtained from Primmbiotech.

Emanuele M., Esposito A., Camerini S., Antonucci F., Ferrara S., Seghezza S., Catelani T., Crescenzi M., Marotta R., Canale C., Matteoli M., Menna E, & Chieregatti E. (2016). Exogenous Alpha-Synuclein Alters Pre- and Post-Synaptic Activity by Fragmenting Lipid Rafts. EBioMedicine, 7, 191-204.

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Adipocyte Size and Inflammation Analyses

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Tissues were fixed in neutral buffered formalin, embedded in paraffin, and sectioned at 5 μm onto poly‐l‐lysine‐coated slides. For histology, sections were stained with H&E. Adipocyte cell size was determined with ImageJ software (US National Institutes of Health), and at least 400 cells were measured from each sample. For immunohistochemistry, deparaffinized sections were immunostained with polyclonal rabbit anti‐mouse primary antibody to PPAR‐α (1:400) (Cell Signaling) according to standard immunohistochemistry procedures. For immunofluorescence analysis, samples were blocked in 5% BSA in PBS and then permeabilized in 0.3% Triton X‐100. Fat samples were incubated with primary antibodies in blocking buffer at 4°C for overnight. After washing, samples were incubated with fluorochrome conjugated secondary antibodies for 1 h at room temperature. Fat pads were imaged on a microscopy (Carl Zeiss Axioplan 2). Anti‐caveolin1 (1:200) and F4/80 (1:200) were purchased from BD Biosciences and Abcam, respectively.

Zhuang H., Wang X., Zha D., Gan Z., Cai F., Du P., Yang Y., Yang B., Zhang X., Yao C., Zhou Y., Jiang C., Guan S., Zhang X., Zhang J., Jiang W., Hu Q, & Hua Z. (2016). FADD is a key regulator of lipid metabolism. EMBO Molecular Medicine, 8(8), 895-918.

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