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Novex tris glycine mini gel

Manufactured by Thermo Fisher Scientific
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The Novex Tris-Glycine Mini-Gel is a pre-cast polyacrylamide gel designed for protein electrophoresis. It is used for the separation and analysis of proteins based on their molecular weight. The gel is prepared with a Tris-Glycine buffer system and is available in various percentage compositions to suit different protein separation needs.

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Lab products found in correlation

Pvdf membrane, by Thermo Fisher Scientific (2 mentions) Hrp conjugated secondary antibody, by Santa Cruz Biotechnology (2 mentions) Halt protease inhibitor cocktail, by Thermo Fisher Scientific (2 mentions) Goat anti rabbit hrp, by Abcam (1 mentions) Nupage novex 3 8 tris acetate protein gel, by Thermo Fisher Scientific (1 mentions) Anti v5, by Thermo Fisher Scientific (1 mentions) Anti ripk3, by Novus Biologicals (1 mentions) Anti actin, by Merck Group (1 mentions) Protease inhibitor cocktail, by Cell Signaling Technology (1 mentions) Supersignal west pico plus chemiluminescent substrate, by Thermo Fisher Scientific (1 mentions) Pvdf membrane, by Merck Group (1 mentions) Cleaved caspase 3, by Cell Signaling Technology (1 mentions) Chemidoc mp imaging system, by Bio-Rad (1 mentions) Gapdh, by GeneTex (1 mentions) Criterion tgx precast midi protein gel, by Bio-Rad (1 mentions) Aβ42 peptide, by Merck Group (1 mentions) Ge10600002, by Cytiva (1 mentions) Anti flag m2 antibody, by Merck Group (1 mentions) Anti β actin, by Merck Group (1 mentions) Protease inhibitor, by Roche (1 mentions)

Close spelling variants of this product

Novex WedgeWell 8–16% Tris–Glycine Mini Gels Novex™ 4–12% Tris-Glycine Mini Gels Novex WedgeWell 14% Tris-Glycine Mini Protein Gels Novex WedgeWell 4–12% Tris-Glycine Mini Gels Novex 16% Tris-Glycine Mini Gels Novex™ WedgeWell™ 4–20% Tris-Glycine Mini Gels Tris-Glycine gels Novex gels Mini-gels Glycine

6 protocols using novex tris glycine mini gel

1

Quantifying Viral Protein Production

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VP and VLP production from 293T cells was monitored for transfection efficiency by p24 ELISA assay, provided under an MTA by the AIDS Vaccine Program, National Cancer Institute (NCI) at Frederick, MD, USA. A radioactive RT assay was also used to measure VP and VLP levels in cell-free supernatants as described previously.18 (link) Viral proteins in formulations were also analyzed by western blot using NuPAGE Novex 3–8% Tris–Acetate Protein Gels (Thermo-Fischer Scientific) and a 1:100 dilution of heat-inactivated serum derived from SHIV-infected macaques, before addition of a 1:2000 dilution of goat anti-monkey IgG: horseradish peroxidase (HRP) (Bio-Rad). Samples were then developed with 3,3′-diaminobenzidine (DAB) SK-4100 (Vector Laboratories). For anti-p17 western blots, a 10–20% Novex Tris-Glycine Mini-Gel (Thermo Fisher, Ca) was used. Membranes were blocked and then stained for 2 h with 1:5000 dilution of polyclonal rabbit anti-p17 antibodies (NIH AIDS Reagent Program), The membrane was then incubated with goat anti-rabbit HRP (Abcam) at 1:2000 concentration and developed using DAB Liquid Substrate (Vector Laboratories).
Pankrac J., Klein K., McKay P.F., King D.F., Bain K., Knapp J., Biru T., Wijewardhana C.N., Pawa R., Canaday D.H., Gao Y., Fidler S., Shattock R.J., Arts E.J, & Mann J.F. (2018). A heterogeneous human immunodeficiency virus-like particle (VLP) formulation produced by a novel vector system. NPJ Vaccines, 3, 2.
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2

SDS-PAGE Analysis of Protein-AuNPs

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Proteins immobilized on AuNPs (1.5
× 1011 particles) were mixed with 20 μL of Novex
Tris-Glycine SDS buffer (1X Thermo Scientific), 5 μL of NuPAGE
reducing buffer (10x, Thermo Scientific), and 10 μL of Milli-Q
water. The mixture was boiled for 2 min at 95 °C. Treated samples
were then loaded in Novex Tris-Glycine MiniGel of 10 wells 4–20%
(Thermo Scientific), and the gels were run for 45 min at 120 mV in
Novex Tris-Glycine SDS (1X) running buffer. Staining was performed
with Coomassie Blue (Aldrich) for 2 h, followed by washing in Milli-Q
water for 3–4 d. Proteins adsorbed onto AuNPs were quantified
by using ImageJ.
Mosquera J., García I., Henriksen-Lacey M., Martínez-Calvo M., Dhanjani M., Mascareñas J.L, & Liz-Marzán L.M. (2020). Reversible Control of Protein Corona Formation on Gold Nanoparticles Using Host–Guest Interactions. ACS Nano, 14(5), 5382-5391.
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3

RIPK3 Western Blot Protocol

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Cells were lysed in NP-40 lysis buffer (150 mM NaCl, 20 mM tris-Cl, 1 mM EDTA, 1% NP-40 at pH 7.5) with 1X Halt Protease Inhibitor Cocktail (Thermo Fisher). 30 μg of protein was run on a 4%−20% Novex Tris-Glycine mini gel (Fisher) at 125 V for 2 h in WB running buffer (24 mM tris, 32 mM glycine, 3.5 mM SDS) and transferred onto PVDF membrane (Thermo Fisher) at 300 mAmpsfor 1 h in transfer buffer (6 mM tris, 8 mM glycine, 15% methanol). Membranes were blocked in 5% dry milkinTBS-Tween20 (1%) for 30 min at room temperature. Membranes were incubated overnight at 4°C with primary anti-RIPK3 (Novus Biologicals), anti-V5 (Thermo Fisher) or anti-actin (EMD Millipore), followed by staining with HRP-conjugated secondary antibodies (Santa Cruz). Membranes were developed using ECL Western Blotting Substrate (Pierce) and film.
Orozco S.L., Daniels B.P., Yatim N., Messmer M.N., Quarato G., Chen-Harris H., Cullen S.P., Snyder A.G., Ralli-Jain P., Frase S., Tait S.W., Green D.R., Albert M.L, & Oberst A. (2019). RIPK3 Activation Leads to Cytokine Synthesis that Continues after Loss of Cell Membrane Integrity. Cell reports, 28(9), 2275-2287.e5.
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4

Immunoblotting Procedure with FKBP Detection

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Cells were lysed in NP40 lysis buffer (150mM NaCl, 20mM Tris-Cl, 1mM EDTA, 1% NP40 at pH 7.5) containing 1X Halt™ Protease Inhibitor Cocktail (ThermoFisher). Thirty μg of protein were run on a 4–12% Novex™ Tris-Glycine mini gel (Fisher Scientific) at 100V for 2.5 hours in WB running buffer (24mM tris, 32mM Glycine, 3.5mM SDS) and transferred onto PVDF membrane (ThermoFisher) at 300mAmps for 50 min in transfer buffer (6mM tris, 8mM glycine). Membrane was blocked in 5% reconstituted dry milk in TBS+1% Tween-20 (TBS-T) for 1 hour. Membranes were stained overnight at 4C with primary anti-FKBP (ThermoFisher PA1-026A) and anti-actin (Millipore MAP1501) antibodies in 1% milk in TBS-T. Membranes were then stained with HRP-conjugated secondary antibodies (Santa Cruz sc-2003) for 1h at room temperature. Membranes were developed on film after treating with Pierce ECL Western Blotting Substrate (Pierce).
Daniels B.P., Snyder A.G., Olsen T.M., Orozco S., Oguin TH I.I.I., Tait S.W., Martinez J., Gale M J.r., Loo Y.M, & Oberst A. (2017). RIPK3 restricts viral pathogenesis via cell death-independent neuroinflammation. Cell, 169(2), 301-313.e11.
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5

Protein Extraction and Western Blot Analysis

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Cells were lysed with NETN300 buffer (1% NP40, 300 mM NaCl, 0.1 mM EDTA, and 50 mM Tris [pH 7.5]) supplemented with protease inhibitor cocktail (Cell Signaling). For TOP1 degradation, cells were incubated in alkaline lysis buffer (200 mM NaOH, 2 mM EDTA), and samples neutralized with neutralization buffer (1M HCl, 600 mM Tris, pH8.0). Subsequently, cell lysates were incubated in nuclease digestion buffer (5 mM CaCl2, 50 mM Tris-HCl, pH8.0). After adding SDS-PAGE sample buffer or 2X boiling lysis buffer (50 mM Tris-HCl pH6.8, 2% SDS, 850 mM β-mercaptoethanol), samples were resolved by SDS-PAGE gels (Novex Tris-Glycine Mini Gels, Invitrogen) and transferred onto PVDF membranes (Millipore). Membranes were immunoblotted with the following antibodies: TOP1 (#556597, BD Biosciences), GAPDH (GTX100118; GeneTex), PARP (9542; Cell signaling), and cleaved caspase-3 (9661; Cell signaling). After overnight incubation, membranes were incubated with the species-appropriate horseradish peroxidase (HRP)-conjugated secondary antibodies for 1 h. Protein signals were visualized by ChemiDoc MP Imaging System (Bio-Rad) with SuperSignal™ West Pico PLUS Chemiluminescent Substrate (Thermo Scientific). Signal intensity was quantified with the Image J software.
Jo U., Murai Y., Agama K.K., Sun Y., Saha L.K., Yang X., Arakawa Y., Gayle S., Jones K., Paralkar V., Sundaram R.K., Doorn J.V., Vasquez J.C., Bindra R.S., Choi W.S, & Pommier Y. (2022). TOP1-DNA trapping by exatecan and combination therapy with ATR inhibitor. Molecular cancer therapeutics, 21(7), 1090-1102.
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6

Quantitative Western Blot Analysis

Cited 1 time
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Protein lysates were prepared with RIPA Buffer (50 mM Tris-HCl pH 8.0, 150 mM NaCl, 1% (v/v) NP40, 0.1% (w/v) SDS, 0.5% (w/v) Na-deoxycholate, protease inhibitor [4693132001, Roche, Basel, Switzerland], and PhosSTOP Phosphatase Inhibitor [4906845001, Roche, Basel, Switzerland]). Aliquots representing 40 µg total protein were separated on 4 to 20% Novex Tris-Glycine Mini Gels (XP04205BOX, Invitrogen, Carlsbad, CA, USA) or 4–20% Criterion™ TGX™ Precast Midi Protein Gel (5671094, Bio-Rad, Hercules, CA, USA) and transferred to 0.2 µm nitrocellulose membranes (GE10600002, Amersham, Little Chalfont, UK). Immunoblotting was performed with anti-β-amyloid antibody (clone WO2, MABN10, Sigma-Aldrich, St. Louis, Missouri, USA) (β-Amyloid [D54D2] XP® Rabbit mAb #8243, Cell Signaling Technology, Danvers, MA, USA), monoclonal ANTI-FLAG M2 antibody (F3165, Sigma-Aldrich, St. Louis, MO, USA), and anti-β-actin (A5441, Sigma-Aldrich, St. Louis, Missouri, USA) antibody as previously described [57 (link)]. A polyclonal antibody against Aβ175 (Anti-Aβ175) was raised in rabbit with the unique peptide (CFRKSKTIQMTSWPT) as antigenic determinant by GenScript (Piscataway, NJ, USA). Aβ42 peptide (A9810, Sigma-Aldrich, St. Louis, MO, USA) was dissolved in DMSO. Quantitative analysis was performed with ImageJ (NIH).
Mo D., Li X., Raabe C.A., Rozhdestvensky T.S., Skryabin B.V, & Brosius J. (2020). Circular RNA Encoded Amyloid Beta peptides—A Novel Putative Player in Alzheimer’s Disease. Cells, 9(10), 2196.
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