Anti fas

Manufactured by Merck Group

Sourced in United States

Anti-Fas is a laboratory instrument used for the detection and quantification of Fas receptor expression on the surface of cells. It functions by utilizing fluorescently labeled antibodies that bind to the Fas receptor, allowing for the analysis of Fas expression levels through flow cytometry or other compatible techniques.

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5 protocols using anti fas

Apoptosis Signaling Pathway Analysis

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The chemicals utilized during study: ammonium sulphate, 2,4-dinitro-phenyl-hydrazine, 1-chloro-2,4-dinitrobenzene, ethylenediaminetetra acetic acid, 5,5-di-thio-bi(2-nitrobenzoic acid), N-ethylmaleimide, nitro blue tetrazolium, reduced nicotinamide adenine dinucleotide, potassium dihydrogen phosphate, phenazinemethosulphate, sodium pyrophosphate, reduced glutathione, sodium azide, thiobarbituric acid, 5-thio-2-nitrobenzoic acid and trichloro acetic acid were procured from Sisco Research Laboratory, India. Bovine serum albumin, Bradford reagent and Pb-acetate were purchased from Sigma-Aldrich, St. Louis, USA. All primary antibodies (produced in rabbit) viz. anti-Bcl-2 (dilution 1:1000), anti-Bad (dilution 1:3000), anti-Cyt C (dilution 1:1000), anti-Apaf-1 (dilution 1:1000), anti-caspase 3 (dilution 1:1000), anti-caspase 8 (dilution 1:1000), anti-caspase 9 (dilution 1:1000), anti-Fas (dilution 1:2000), anti-Bid (dilution 1:1000) and anti-actin (dilution 1:3000) for immunoblotting were purchased from Sigma-Aldrich Chemical Company St. Louis, USA. Appropriate HRP conjugated secondary antibody (dilution 1:3000) produced in goat was also purchased from Sigma-Aldrich Chemical Company St. Louis, USA. Methanol, formic acid, acetic acid and acetonitrile were obtained from Merck, India.

Dewanjee S., Dua T.K., Khanra R., Das S., Barma S., Joardar S., Bhattacharjee N., Zia-Ul-Haq M, & Jaafar H.Z. (2015). Water Spinach, Ipomoea aquatica (Convolvulaceae), Ameliorates Lead Toxicity by Inhibiting Oxidative Stress and Apoptosis. PLoS ONE, 10(10), e0139831.

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Protein Expression Analysis of HosDXR150 Cells

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Treated and untreated HosDXR150 cells were lysed in 50 mM Tris/HCl, 5 mM EDTA, 250 mM NaCl, 50 mM NaF, 0.1% Triton-X, 0.1 mM Na₃VO₄ plus protease inhibitors (Roche Molecular Biochemicals, Germany). Equal amounts of proteins were resolved on a 7% or 10% SDS-PAGE, transferred onto nitrocellulose membranes, and then successively blocked with 5% non-fat dry milk. Anti-RBL2 was from BD Transduction Laboratories. Anti-FAS, anti-CASP10 and anti-IL12A were from Sigma-Aldrich. Anti-TP73, anti-TP53, anti-actin and the horseradish peroxidase secondary antibodies were from Santa Cruz Biotechnology. Primary antibodies were used at a dilution of 1∶200. Secondary antibodies were used at a dilution of 1∶5000. Signals were acquired using the ImageQuant LAS 4000 (GE Healthcare).

Capobianco E., Mora A., La Sala D., Roberti A., Zaki N., Badidi E., Taranta M, & Cinti C. (2014). Separate and Combined Effects of DNMT and HDAC Inhibitors in Treating Human Multi-Drug Resistant Osteosarcoma HosDXR150 Cell Line. PLoS ONE, 9(4), e95596.

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Western Blot Analysis of FAIM2, Fas, and Caspase 8

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Whole cell lysates were prepared from cell lines (H460, H1703, A549, H128, H209, and H889) with RIPA lysis buffer. Western blot analysis was performed using 50 μg of protein extracts per lane, electrophoresed, transferred to PVDF membranes (Millipore), and immunoblotted with anti-FAIM2 (Novus), anti-Fas (Milipore), caspase 8 (Cell Signaling Technology), and anti-β-actin (AC–15, Sigma). The membranes were washed and treated with rat anti-species IgG secondary antibody conjugated to horseradish peroxidase (Amersham Pharmacia). The antigen -antibody reactions were visualized by using enhanced chemiluminescence assay ECL (Amersham Pharmacia) and exposed to enhanced chemiluminescence film.

Kang H.C., Kim J.I., Chang H.K., Woodard G., Choi Y.S., Ku J.L., Jablons D.M, & Kim I.J. (2016). FAIM2, as a novel diagnostic maker and a potential therapeutic target for small-cell lung cancer and atypical carcinoid. Scientific Reports, 6, 34022.

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Monoclonal Antibody-Induced Apoptosis Assay

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The monoclonal agonist antibody against CD95 (Anti-Fas) was purchased from Millipore (Bedford, MA). Caspase-8 deficient Jurkat cells were kind gift from Dr. Junying Yuan at Harvard University. HeLa cells were obtained from Cellbank (Shanghai, China). Jurkat cells were cultured in RPMI1640 and HeLa cells were cultured in DMEM (Corning, Manassas, VA), supplemented with 10% fetal bovine serum (PAN-Biotech, Aidenbach, Germany). All the other biochemical reagents were from Sigma Aldrich.

Shen C., Pei J., Guo X., Zhou L., Li Q, & Quan J. (2018). Structural basis for dimerization of the death effector domain of the F122A mutant of Caspase-8. Scientific Reports, 8, 16723.

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Quantifying Protein S-Glutathionylation in Lung Tissue

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Overall protein S-glutathionylation in lung tissue was assessed quantitatively following tissue homogenization, precipitation of proteins with 0.6% sulfosalicylic acid, and release of GSH with 1% NaBH₄. GSH was quantitated using the 5,5’-dithio-bis(2-nitrobenzoic acid) (DTNB)–GSSG reductase recycling method⁵². To detect S-glutathionylation of FAS or GLRX, lung lysates were prepared (50 mM Tris, pH 7.4, 150 mM NaCI, 0.25% SDS, 1% NP-40, 0.5% CHAPS, and 20 mM N-ethylmaleimide with protease inhibitor cocktail [Sigma-Aldrich]), and protein content was equalized. 2 μg/ml antiglutathione antibody (American Diagnostica) was added to immunoprecipitate S-glutathionylated proteins using protein G agarose beads. Samples were analyzed by immunoblotting using anti-FAS (Millipore) or anti-GLRX (Virogen) antibodies. As a control, a portion of the lysate was treated with 50 mM DTT to reduce glutathionylated proteins, and these samples were purified through columns (Bio-Rad) to remove DTT before subsequent IP.

Anathy V., Lahue K.G., Chapman D.G., Chia S.B., Casey D.T., Aboushousha R., van der Velden J.L., Elko E., Hoffman S.M., McMillan D.H., Jones J.T., Nolin J.D., Abdalla S., Schneider R., Seward D.J., Roberson E.C., Liptak M.D., Cousins M.E., Butnor K.J., Taatjes D.J., Budd R.C., Irvin C.G., Ho Y.S., Hakem R., Brown K.K., Matsui R., Bachschmid M.M., Gomez J.L., Kaminski N., van der Vliet A, & Janssen-Heininger Y.M. (2018). Reducing protein oxidation reverses lung fibrosis. Nature medicine, 24(8), 1128-1135.

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