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Swift membrane stain

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Swift Membrane Stain is a laboratory reagent used for the staining and visualization of cell membranes. It provides a simple and effective method for labeling and imaging cell surface structures. The stain binds to lipid bilayers, allowing for the clear delineation of cellular boundaries under microscopic examination.

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Lab products found in correlation

Anti p smad2, by Abcam (2 mentions) Anti smad2 3, by Cell Signaling Technology (2 mentions) Anti collagen 1, by Abcam (2 mentions) Anti tgf β, by R&D Systems (2 mentions) Anti tric b, by Thermo Fisher Scientific (2 mentions) Anti hsp47, by Santa Cruz Biotechnology (2 mentions) Anti psmad3 phospho s423 s425, by Rockland Immunochemicals (2 mentions) Anti β actin antibody, by Santa Cruz Biotechnology (2 mentions) Anti p camkii, by Abcam (2 mentions) Rc dc protein assay, by Bio-Rad (2 mentions) Imagequant las 4000, by GE Healthcare (2 mentions) Anti gapdh, by Cell Signaling Technology (2 mentions) Anti p smad3, by Abcam (2 mentions) Lipofectamine 2000, by Thermo Fisher Scientific (2 mentions) Protease and phosphatase inhibitor, by Merck Group (1 mentions) Supersignal west dura, by Thermo Fisher Scientific (1 mentions) Criterion system, by Bio-Rad (1 mentions) Glua2 3, by Merck Group (1 mentions) Camkiiα, by Merck Group (1 mentions) Gapdh, by Cell Signaling Technology (1 mentions)

6 protocols using swift membrane stain

1

Protein Extraction and Analysis from Mouse Brains

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Mouse brains were extracted rapidly on ice and then sliced into 1 mm sections, and dorsal hippocampus was removed with a 12 gauge punch and immediately frozen on dry ice. Both human and mouse samples were homogenized by light sonication in modified RIPA buffer (10 mM Tris base, 150 mM sodium chloride, 1 mM EDTA, 0.1% sodium dodecyl sulfate, 1% Triton X-100, 1% sodium deoxycholate, pH 7.4, protease and phosphatase inhibitors [Sigma Aldrich]). Concentration was measured using DC Protein Assay (BioRad) and gel samples were normalized for total protein. Proteins were separated on 4–15% polyacrylamaide gradient gels (Criterion System, BioRad), and Western blotting was performed using chemiluminescence (SuperSignal West Dura, Thermo Scientific). Total protein was assayed using Swift Membrane Stain (G Biosciences) and proteins were quantified using ImageJ software (NIH). Primary antibodies were used to detect FosB isoforms (5G4; 1:500; Cell signaling, 2251), GluA2/3 (1:1,000; Millipore, 07–598), CaMKIIα (1:1,000; Millipore, 05–532), cdk5 (1:1,000; Santa cruz, sc-173), GAPDH (1:20,000; Cell Signaling, 21185).
Gajewski P.A., Turecki G, & Robison A.J. (2016). Differential Expression of FosB Proteins and Potential Target Genes in Select Brain Regions of Addiction and Depression Patients. PLoS ONE, 11(8), e0160355.
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2

Evaluating mGluR2 Expression in Nucleus Accumbens

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To investigate whether mGluR2 protein expression was downregulated in the nucleus accumbens shell after two weeks of CIE, a separate cohort of mice underwent ethanol self-administration and CIE exposure following the protocol described above. Mice were sacrificed after two weeks of CIE via rapid decapitation under isoflurane anesthesia. Nucleus accumbens shell was microdissected from tissue, sonicated in LDS, and stored at −20 °C until Western blot analysis. After transfer, total protein was assessed using Swift Membrane Stain (G-Biosciences). Membranes were probed using a selective mouse anti-mGluR2 antibody (Abcam; 1:1000) and visualized using a HRP-conjugated goat anti-mouse secondary antibody (Southern Biotech; 1:5000) with BioRad high-sensitivity ECL. mGluR2 protein was normalized to total protein to control for loading.
Barker J.M., Lench D.H, & Chandler L.J. (2015). Reversal of alcohol dependence-induced deficits in cue-guided behavior via mGluR2/3 signaling in mice. Psychopharmacology, 233(2), 235-242.
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3

Antibody Production and Reagent Sources

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Reagents were purchased from the following suppliers: oligonucleotides, Lipofectamine 2000, cell culture reagents, Alexa Fluor 647- and HRP-conjugated goat anti-rabbit IgG, and MitoTracker Orange CMTMRos from Thermo Fisher Scientific; restriction enzymes from New England Biolabs; HEK293 and HEK293T cells from the American Type Culture Collection; Swift membrane stain from G-biosciences. Antibodies against glyceraldehyde-3-phosphate dehydrogenase (GAPDH), citrate synthase, and catalase were purchased from Cell Signaling. The Nudt7 antibody was generated as previously described (19 (link)). 3’,5’-ADP and antibodies against ATP-binding cassette, sub-family D, member 3 (PMP70) and the FLAG epitope were obtained from Sigma-Aldrich; the Dylight 488 mouse IgG was purchased from Rockland Immunochemicals. The antibody against the full-length mouse Nudt8 was raised in rabbit and purified by antigen affinity chromatography. The fluorescent CoA derivative of monobromobimane (mBB), mBB-CoA, was synthesized as previously described (13 (link)). All other reagents were of analytical grade or better and were purchased from Sigma-Aldrich or Fisher Scientific, unless otherwise stated.
Kerr E.W., Shumar S.A, & Leonardi R. (2019). Nudt8 is a novel CoA diphosphohydrolase that resides in the mitochondria. FEBS letters, 593(11), 1133-1143.
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4

FtsN Protein Immunoblotting Protocol

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Samples from the FtsN depletion strain were collected as described above and separated by SDS-PAGE, using equal volumes of normalized samples per lane. Using a wet apparatus, FLAG-tagged proteins were transferred onto a nitrocellulose membrane and stained with Swift membrane stain (G-Biosciences; St. Louis, MO) to show that similar levels of proteins in all lanes were loaded and transferred. The membrane was immunoblotted with mouse monoclonal anti-FLAG antibody (1:5,000) and goat anti-mouse secondary antibody conjugated to horseradish peroxidase (HRP; 1:10,000). HRP was detected using Western Lightning ECL Pro (PerkinElmer, Inc., Waltham, MA) and quantified using Image Studio Software (LI-COR; Lincoln, NE).
Busiek K.K, & Margolin W. (2014). A role for FtsA in SPOR-independent localization of the essential Escherichia coli cell division protein FtsN. Molecular microbiology, 92(6), 1212-1226.
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5

Quantitative Western Blot Analysis of Bone Cell Signaling

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Protein lysates were obtained from minced bones and from OBs using RIPA lysis buffer supplemented with protease inhibitors as previously described(47 (link)). Following protein quantitation using RC DC Protein Assay (BioRad), proteins were separated on 6% (collagen), 9% (pSMAD2 and SMAD2/3), 10% (TRIC-B, HSP47) or 15% (TGF-β) SDS-PAGE and transferred on PVDF membrane. The membranes were incubated o/n at 4°C with 1:1000 anti-TRIC-B (Invitrogen), anti-SMAD2/3 (Cell Signaling), anti-pSMAD2 (Abcam), anti-pSMAD3 (Abcam), anti-HSP47 (Santa Cruz) anti-collagen I (Abcam), anti-TGF-b (R&D System), anti-pCaMKII (Abcam) antibodies in TBS-T. ImageQuant LAS 4000 (GE Healthcare) and the ImageQuant LAS 4000 1.2 software were used for images acquisition. ImageQuant TL analysis software was employed for band intensity evaluation. At least biological triplicates were performed. For each gel, the expression of the mutant samples was expressed as fold difference compared to controls. Protein loading normalization was determined using anti-β-actin antibody (Santa Cruz Biotechnology) or total proteins staining by Swift™ Membrane Stain (G-Biosciences). For human cells, the following antibodies and dilutions were used: anti-pSMAD3 (phospho S423/S425) 1:1000 (Rockland) and anti-GAPDH 1 :1000 (Cell Signaling).
Joiner W.J., Wang L.Y., Tang M.D, & Kaczmarek L.K. (1997). hSK4, a member of a novel subfamily of calcium-activated potassium channels. Proceedings of the National Academy of Sciences of the United States of America, 94(20), 11013-11018.
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6

Protein Expression Analysis in Osteoblasts

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Protein lysates were obtained from minced bones and from OBs using RIPA lysis buffer supplemented with protease inhibitors as previously described (47) . Following protein quantitation using RC DC Protein Assay (BioRad), proteins were separated on 6% (collagen), 9% (pSMAD2 and SMAD2/3), 10% (TRIC-B, HSP47) or 15% (TGF-β) SDS-PAGE and transferred on PVDF membrane. The membranes were incubated o/n at 4°C with 1:1000 anti-TRIC-B (Invitrogen), anti-SMAD2/3 (Cell Signaling), anti-pSMAD2 (Abcam), anti-pSMAD3 (Abcam), anti-HSP47 (Santa Cruz) anti-collagen I (Abcam), anti-TGF-b (R&D System), anti-pCaMKII (Abcam) antibodies in TBS-T. ImageQuant LAS 4000 (GE Healthcare) and the ImageQuant LAS 4000 1.2 software were used for images acquisition. ImageQuant TL analysis software was employed for band intensity evaluation. At least biological triplicates were performed. For each gel, the expression of the mutant samples was expressed as fold difference compared to controls. Protein loading normalization was determined using anti-β-actin antibody (Santa Cruz Biotechnology) or total proteins staining by Swift ™ Membrane Stain (G-Biosciences). For human cells, the following antibodies and dilutions were used: anti-pSMAD3 (phospho S423/S425) 1:1000 (Rockland) and anti-GAPDH 1 :1000 (Cell Signaling).
Besio R., Contento B.M., Garibaldi N., Filibian M., Sonntag S., Shmerling D., Tonelli F., Biggiogera M., Brini M., Salmaso A., Jovanovic M., Marini J.C., Rossi A, & Forlino A. (2023). CaMKII inhibition due to TRIC-B loss-of-function dysregulates SMAD signaling in osteogenesis imperfecta. Matrix biology : journal of the International Society for Matrix Biology, 120.
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