Nupage 12 bis tris mini gels

Manufactured by Thermo Fisher Scientific

Sourced in United States

The NuPAGE 12% bis-tris mini gels are pre-cast polyacrylamide gels designed for protein electrophoresis. They have a 12% bis-tris acrylamide concentration and are available in a mini gel format.

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Lab products found in correlation

Simplyblue safestain, by Thermo Fisher Scientific (2 mentions) Mes sds running buffer, by Thermo Fisher Scientific (1 mentions) Xcell surelock mini cell electrophoresis system, by Thermo Fisher Scientific (1 mentions) Novex colloidal blue staining kit, by Thermo Fisher Scientific (1 mentions) Nupage mops sds running buffer 20, by Thermo Fisher Scientific (1 mentions) Perfection v600 photo scanner, by Epson (1 mentions) Pageruler prestained protein ladder, by Thermo Fisher Scientific (1 mentions) Nupage lds sample buffer 4, by Thermo Fisher Scientific (1 mentions) Milli q water, by Merck Group (1 mentions)

Close spelling variants of this product

NuPAGE Bis-Tris 4–12% mini-gels NuPAGE Novex 4–12% or 12% Bis-Tris mini gels NuPage Novex 4–12% Bis-Tris Mini Gels NuPAGE™ 4 to 12% Bis-Tris Mini Protein Gels NuPAGE 12% Bis-Tris gels NuPAGE Bis-Tris Mini Gels NuPAGE Bis-Tris gels NuPAGE 12% Bis-Tris Bis-Tris mini-gels NuPAGE Bis-Tris

6 protocols using nupage 12 bis tris mini gels

Prion Protein Oligomerization Assay

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rPrP was incubated with 50, 250 or 500 μM PE or POPG at room temperature for 16 hours in 20 mM Tris pH 7.5, 135 mM NaCl, 2 mM EDTA and 0.05% Triton. 2X loading buffer (125 mM Tris pH 6.8, 40% Glycerol, 0.02% Bromophenol blue) was added and samples were loaded in NuPAGE 12% Bis-Tris minigels (Novex, Life Technology) without temperature denaturation. Electrophoresis was performed in 1X MES-SDS running buffer (Novex); gels were stained with coomassie blue.
To assess the oligomerization state of rPrP in sucrose density gradient fractions, 10 ul of each fraction was incubated with 2X-sample buffer (125 mM Tris pH 6.8, 40% glycerol, 0.02% Bromophenol blue) for 10 min at room temperature. 10 ul of each fraction was loaded to NuPAGE 12% Bis-Tris minigels (Novex) without temperature denaturation. Electrophoresis was performed in 1X MES-SDS running buffer (Novex), and gels were stained with silver.

Srivastava S, & Baskakov I.V. (2015). Contrasting Effects of Two Lipid Cofactors of Prion Replication on the Conformation of the Prion Protein. PLoS ONE, 10(6), e0130283.

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Protein Separation and Visualization

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Both protein fractions (50 µg per lane) were separated on 10-well NuPAGE 12% Bis-Tris minigels (Thermo Fisher Scientific, Rockford, IL, USA) under reducing conditions. Gels were incorporated in the XCell SureLock™ Mini-Cell Electrophoresis System (Invitrogen, Carlsbad, CA, USA) and prepared with NuPAGE™ MOPS SDS Running Buffer 20× (Thermo Fisher Scientific, Rockford, IL, USA) according to the supplier’s protocol. In addition, 10 µL of the SeabluePlus 2 Pre-Stained Protein Standard (Thermo Fisher Scientific, Rockford, IL, USA) was used as molecular weight reference and separated at 150 V for 1.5 h at 4 °C. After separation, gels were fixed and stained using Novex Colloidal Blue Staining Kit (Thermo Fisher Scientific, Rockford, IL, USA) according to the manufacturer’s instructions. Gels were destained for at least 16 h and scanned using an Epson Perfection V600 Photo Scanner (Seiko Epson Corporation, Suma, Nagano, Japan) at 700 dpi. Protein migration patterns were manually inspected and subjected to further in-gel trypsin digestion.

Schmelter C., Funke S., Treml J., Beschnitt A., Perumal N., Manicam C., Pfeiffer N, & Grus F.H. (2018). Comparison of Two Solid-Phase Extraction (SPE) Methods for the Identification and Quantification of Porcine Retinal Protein Markers by LC-MS/MS. International Journal of Molecular Sciences, 19(12), 3847.

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Milk Protein Profiling by SDS-PAGE

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The individual proteins in the raw milk, centrifugate before and after HHT, and cheese milks were identified by SDS-PAGE. All milk samples were diluted, using Milli-Q water (Millipore, Billerica, MA), to a protein concentration of ~6 µg/µL. A portion of the diluted samples were further diluted with SDS sample buffer [NuPAGE LDS Sample Buffer (4×; Thermo Fisher Scientific, Waltham, MA), composed of lithium salt, glycerine, sulfuric acid, and monododecyl ester]. For reducing SDS-PAGE, samples were treated with dithiothreitol [NuPAGE Sample Reducing Agent (10×); concentration = 500 mmol/L] at a level of 10% (vol/ vol) of the total sample volume mixture. All samples were heated at 70°C for 10 min, cooled, and loaded on SDS-PAGE gels (NuPAGE 12% Bis-Tris mini gels) at a rate of 10 µg/well before running in SDS running buffer [NuPAGE MOPS SDS Running Buffer (1×)] at constant voltage of 200 V for 50 min using Mini Gel Tank (XCell SureLock Mini, Thermo Fisher Scientific). After electrophoresis, the gels were stained as described by McCarthy et al. (2012) (link). The SDS-PAGE gels were scanned using an Epson V700 film scanner (Epson, Suwa, Nagano, Japan). The identities of principal protein bands in the milk samples were determined using prestained protein molecular weight marker (PageRuler Prestained Protein Ladder, 10 to 180 kDa, Thermo Fisher Scientific).

Lamichhane P., Kelly A.L, & Sheehan J.J. (2018). Effect of milk centrifugation and incorporation of high-heat-treated centrifugate on the composition, texture, and ripening characteristics of Maasdam cheese. Journal of dairy science, 101(7).

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Gel Electrophoresis of Protein-Compound Interactions

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10 μM of each protein were incubated at various times with 20 μM of compounds in 25 mM TRIS at pH 8, 150 mM NaCl, 50 μM zinc acetate, and 1 mM DTT buffer. Samples were subjected to gel electrophoresis with SDS-PAGE gel using the NuPAGE 12% bis-tris mini gels (Life Technologies), and MES as running buffer. Gels were subsequently stained with SimplyBlue SafeStain (Life Technologies) according to the manufacture’s protocol.

Gambini L., Baggio C., Udompholkul P., Jossart J., Salem A.F., Perry J.J, & Pellecchia M. (2019). Covalent Inhibitors of Protein-Protein Interactions Targeting Lysine, Tyrosine, or Histidine Residues. Journal of medicinal chemistry, 62(11), 5616-5627.

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Bcl-2 Protein Binding Assay

Cited 1 time

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Synthetic peptides
were incubated for 2 h and at equimolar concentration (10 μM)
with human Bcl-2 family proteins (hBfl-1, hMcl-1, hBcl-2, hBcl-xL).
Note that the paper from Huhn et al. used 40 μM
protein and 120 μM peptides.^{40 (link)} Samples
were subjected to gel electrophoresis with SDS-PAGE gel followed by
treatment with Coomassie dye as a staining protocol. For protein band
detection, the NuPAGE 12% bis-tris mini gels (Life Technologies) were
stained with SymplyBlue SafeStain (Life Technologies) according to
the manufacture’s protocol.

Barile E., Marconi G.D., De S.K., Baggio C., Gambini L., Salem A.F., Kashyap M.K., Castro J.E., Kipps T.J, & Pellecchia M. (2016). hBfl-1/hNOXA Interaction Studies Provide New Insights on the Role of Bfl-1 in Cancer Cell Resistance and for the Design of Novel Anticancer Agents. ACS Chemical Biology, 12(2), 444-455.

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Protein-Compound Binding Assay

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10 μM of each protein were incubated for 10 min with 20 μM of each compound in a buffer composed of 25 mM TRIS at pH 8, 150 mM NaCL, 50 μM zinc acetate, and 1 mM DTT. Samples were subjected to gel electrophoresis with SDS-PAGE gel using the NuPAGE 12% bis-tris mini gels (Life Technologies), MES as running buffer, and were stained with SimplyBlue SafeStain (Life Technologies) according to the manufacture’s protocol.

Baggio C., Gambini L., Udompholkul P., Salem A.F., Aronson A., Dona A., Troadec E., Pichiorri F, & Pellecchia M. (2018). Design of Potent pan-IAP and Lys-Covalent XIAP selective Inhibitors Using a Thermodynamics Driven Approach. Journal of medicinal chemistry, 61(14), 6350-6363.

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