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Nupage 4 10 bis tris polyacrylamide gels

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The NuPAGE® 4%–10% Bis‐Tris polyacrylamide gels are precast electrophoresis gels designed for the separation and analysis of proteins. The gels feature a Bis-Tris buffering system and a 4%–10% gradient of polyacrylamide, which allows for the effective separation of a wide range of protein sizes.

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Lab products found in correlation

Mes sds running buffer, by Thermo Fisher Scientific (2 mentions) Peroxidase conjugated goat anti rabbit antibody, by Thermo Fisher Scientific (2 mentions) Signalfire ecl reagent system, by Cell Signaling Technology (2 mentions) 0.2 μm pvdf membrane, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

Bis-Tris gels (1248 citations) NuPAGE Bis-Tris gels (1245 citations) 4–12% Bis-Tris polyacrylamide gel (166 citations) NuPAGE 10% Bis-Tris gels (95 citations) NuPAGE Bis-Tris (95 citations) NuPAGE Bis-Tris polyacrylamide gels (47 citations) NuPAGE polyacrylamide gels (13 citations) NuPAGE 10% Bis-Tris (9 citations) NuPAGE 10% Bis-Tris polyacrylamide gels (8 citations) NuPAGE 10% polyacrylamide - Bis-Tris gel (2 citations)

2 protocols using nupage 4 10 bis tris polyacrylamide gels

1

Western Blot Analysis of Cyanobacterium-Virus Interactions

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Samples were resolved on precast NuPAGE® 4%–10% Bis‐Tris polyacrylamide gels in MES SDS running buffer (Life Technologies, Grand Island, NY) under reducing conditions according to the manufacturer's instructions. Proteins were visualized by Coomassie Blue staining or transferred to 0.2 μm PVDF membrane (Invitrogen, Grand Island, NY) for standard Western blotting: primary antibody was polyclonal rabbit anti‐CV‐N antibodies (Molecular Targets Laboratory, CCR, NCI, NIH, Bethesda, MD) used at 1 : 1500 dilution (overnight incubation), and secondary antibody was peroxidase‐conjugated goat anti‐rabbit antibody (Thermo Fisher Scientific Inc.) used at 1:2000 for 1 h. Western blot was detected using the SignalFire ECL reagent system (Cell Signaling Technology Inc., Boston, MA).
O'Keefe B.R., Murad A.M., Vianna G.R., Ramessar K., Saucedo C.J., Wilson J., Buckheit K.W., da Cunha N.B., Araújo A.C., Lacorte C.C., Madeira L., McMahon J.B, & Rech E.L. (2015). Engineering soya bean seeds as a scalable platform to produce cyanovirin‐N, a non‐ARV microbicide against HIV. Plant Biotechnology Journal, 13(7), 884-892.
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2

Protein Expression Analysis by Western Blot

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Samples were resolved on pre-cast NuPAGE® 4–10% Bis-Tris polyacrylamide gels in MES SDS running buffer (Life Technologies, USA) under reducing conditions according to the manufacturer’s instructions. Proteins were visualized by Coomassie Blue staining or transferred to 0.2 µm PVDF membrane (Invitrogen, USA) for standard western blotting: primary antibody was polyclonal rabbit anti-CV-N antibodies (NIH, USA) used at 1:1,500 dilution (overnight incubation), and secondary antibody was peroxidase-conjugated goat anti-rabbit antibody (Thermo Fisher Scientific Inc., USA) used at 1:2000 for 1h. Western blot was detected using the SignalFire ECL reagent system (Cell Signaling Technology Inc., USA).
O'Keefe B.R., Murad A.M., Vianna G.R., Ramessar K., Saucedo C.J., Wilson J., Buckheit K.W., da Cunha N.B., Araújo A.C., Lacorte C.C., Madeira L., McMahon J.B, & Rech E.L. (2015). Engineering soya bean seeds as a scalable platform to produce cyanovirin‐N, a non‐ARV microbicide against HIV. Plant Biotechnology Journal, 13(7), 884-892.
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