Tris glycine gel

Manufactured by Lonza

Sourced in United States

Tris-Glycine gel is a type of electrophoresis gel used to separate and analyze proteins based on their molecular weight. It consists of a polyacrylamide matrix that is buffered with Tris-Glycine solution. The gel provides a stable and consistent medium for protein separation and can be used in various electrophoresis techniques, such as SDS-PAGE.

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Lab products found in correlation

Ripa buffer, by Thermo Fisher Scientific (2 mentions) Pierce bca protein assay kit, by Thermo Fisher Scientific (2 mentions) Tween 20, by Thermo Fisher Scientific (1 mentions) Supersignal west pico chemiluminescence substrate, by Thermo Fisher Scientific (1 mentions) Chemidoc xrs system, by Bio-Rad (1 mentions) Immobilon pvdf membrane, by Merck Group (1 mentions) Anti actin, by Merck Group (1 mentions) Rabbit monoclonal anti p21, by Cell Signaling Technology (1 mentions) Mouse monoclonal anti actin, by Abcam (1 mentions) Rabbit polyclonal anti parp, by Cell Signaling Technology (1 mentions) Mouse monoclonal anti p53 sc 126, by Santa Cruz Biotechnology (1 mentions) Rabbit polyclonal anti caspase 3, by Cell Signaling Technology (1 mentions) Odyssey infrared imaging system, by LI COR (1 mentions) Anti β actin, by Merck Group (1 mentions) Nitrocellulose membrane, by Bio-Rad (1 mentions) Protease inhibitor tablet, by Roche (1 mentions) Odyssey fluorescent scanner, by LI COR (1 mentions) Grip1, by BD (1 mentions) Gapdh, by Cell Signaling Technology (1 mentions) Irdye 680, by LI COR (1 mentions)

Spelling variants of this product

4 – 20% Tris-Glycine gels (7 citations) 4–20% Tris-Glycine gradient gels (6 citations)

5 protocols using tris glycine gel

Western Blot Analysis of Cell Signaling

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For cell extracts, cells were lysed in RIPA buffer (Thermo) containing protein and phosphatase inhibitor cocktail (Cell Signaling Technologies, Danvers, MA) for 30 min on ice. Samples were clarified by centrifugation at 14,000 x g for 20 min at 4 °C. Supernatants were collected, mixed with Laemmli sample buffer, separated on 4–20% TRIS-glycine gels (Lonza), and transferred to PVDF membrane (EMD) and blocked, as described previously [4 (link), 37 (link)]. Membranes were incubated overnight at 4 °C with a 1/1000 dilution of rabbit antibodies against active caspase 3, phosphorylated ERK, PTEN (Cell Signaling Technology) or 500 ng/ml anti-mouse actin (Genscript, Piscataway, NJ). Membranes were washed in TBS/ 0.1% (v/v) Tween 20 (Thermo). Antibodies were detected with 1 μg/ml peroxidase conjugated goat Fab₂ anti-rabbit or anti-mouse antibodies (Jackson ImmunoResearch), as described previously [4 (link)]. SuperSignal West Pico Chemiluminescence Substrate (Thermo) was used following the manufacturer’s protocol to visualize the peroxidase using a ChemiDoc XRS+ System (BioRad Hercules, CA).

Chen W., Pilling D, & Gomer R.H. (2017). C-reactive protein (CRP) but not the related pentraxins serum amyloid P and PTX3 inhibits the proliferation and induces apoptosis of the leukemia cell line Mono Mac 6. BMC Immunology, 18, 47.

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Protein Isolation and Western Blot

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Cells were treated with vehicle, quarfloxin, or CX-5461 as indicated. At harvesting, floating cells and adherent cells (trypsination) were collected for analysis. Protein isolation and blotting were performed essentially as previously described using NuPAGE 4–12% bis-tris precast polyacrylamide gels and Immobilon-PVDF membranes (Millipore) [42 (link)]. For western blots containing Caspase-3 and p21, 4–20% Tris-Glycine gels (Lonza) were used for better separation of these low MW proteins. Primary antibodies used in this study were mouse monoclonal anti-MycN (sc-53993, Santa Cruz Biotechnology, CA, USA), mouse monoclonal anti-p53 (sc-126, Santa Cruz Biotechnology, CA, USA), rabbit monoclonal anti-p21 (#2947, Cell Signaling Technology, MA, USA), rabbit polyclonal anti-PARP (#9542, Cell Signaling Technology, MA, USA), rabbit polyclonal anti-Caspase-3 (#9662, Cell Signaling Technology, MA, USA), mouse monoclonal anti-γ-H2A.X (05–636, Merck Millipore, MA, USA), rabbit polyclonal anti-actin (A2066, Sigma-Aldrich, MO, USA) and mouse monoclonal anti-actin (AB3280, Abcam, Cambridge, UK). Membranes were detected using the Odyssey Infrared Imaging system (LI-COR).

Hald Ø.H., Olsen L., Gallo-Oller G., Elfman L.H., Løkke C., Kogner P., Sveinbjörnsson B., Flægstad T., Johnsen J.I, & Einvik C. (2018). Inhibitors of ribosome biogenesis repress the growth of MYCN-amplified neuroblastoma. Oncogene, 38(15), 2800-2813.

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Pfs25 Binding and Characterization with Hydroxocobalamin

Cited 2 times

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His-tagged Pfs25, prepared from a Baculovirus system as previously described [31 (link)], was diluted to 80 µg/mL and incubated with varying amounts of hydroxocobalamin hydrochloride. At the optimum binding ratio, hydroxocobalamin hydrochloride (320 µg/mL) was incubated with 80 µg/mL Pfs25 at different time points and then subjected to native electrophoresis using Tris-Glycine gel (Lonza, Basel, Switzerland). Hydroxocobalamin acetate (Sigma-Aldrich # H8017) and cyanocobalamin were also incubated with Pfs25 for comparison at 1:4 Pfs25:Cbl/CoPoP binding ratio. For peptide binding, a fluorescently labeled peptide, FAM-RGD, was used and was previously demonstrated to bind to CoPoP liposomes [14 (link)].

Federizon J., Feugmo C.G., Huang W.C., He X., Miura K., Razi A., Ortega J., Karttunen M, & Lovell J.F. (2021). Experimental and Computational Observations of Immunogenic Cobalt Porphyrin Lipid Bilayers: Nanodomain-Enhanced Antigen Association. Pharmaceutics, 13(1), 98.

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Western Blot Analysis of Ion Channels

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Pooled limb tissues from at least five embryos were lyzed in RIPA lysis buffer (50 mM Tris, 150 mM NaCl, 0.1% SDS, 0.5% sodium deoxycholate, and 1% NP40) with protease inhibitor tablet (Roche, Indianapolis, IN, USA). The protein concentration was measured using Bio-Rad reagents. Proteins (20 μg) were loaded to the pre-casted 4%–12% of tris-glycine gel (Lonza, Allendale, NJ, USA), and the proteins were separated at 100 V for about 100 minutes. Protein samples were then transferred onto nitrocellulose membranes (Bio-Rad, Hercules, CA, USA) at 220 mA for 3 hours at 4 ° C. After being blocked, membranes were incubated with primary antibody on a rotator shaker in a cold room overnight. Blots were then incubated by a species-specific horseradish peroxidase-labeled secondary antibody and developed using chemiluminescent substrate (Pierce, Rockford, IL, USA). The actb protein expression served as an endogenous control. Primary antibodies used were: kcna6 (Kv1.6; Alomone, Cat number APC-003, Jerusalem 91042 Israel), kcnh2 (Kv11.1; abcam, Cat number: ab81160, Cambridge, MA, USA), kcnj8 (Kir6.1; Sigma, Cat number: P0874, St. Louis, MO, USA), and anti-β-actin (actb; Sigma, Cat number: A2228).

Zhang W., Das P., Kelangi S, & Bei M. (2019). Potassium channels as potential drug targets for limb wound repair and regeneration. Precision Clinical Medicine, 3(1), 22-33.

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Quantifying GRIP1 in Prefrontal Cortex

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GRIP1 levels in the prefrontal cortex were measured using a western blot, as described in Briand et al., 2014 (link). Briefly, animals were decapitated, and the prefrontal cortex dissected using a brain block (Braintree Scientific). Protein quantification was performed using a Pierce BCA Protein Assay Kit (Thermo Scientific). Equal amounts of protein (30 µg) were loaded into each well of a Tris-glycine gel (Lonza) and transferred to nitrocellulose membranes (Immobilon). Membranes were blocked with Li-Cor blocking buffer and allowed to incubate in primary antibody solution (GRIP1, 1:2000 (BD Biosciences) and GAPDH, 1:5000 (Cell Signaling)) for 24 hours at 4°C. Membranes were then incubated with fl uorescent secondary antibodies (1:20,000; IR-dye 680 or IR-dye 800, Li-Cor) and imaged on an Odyssey fluorescent scanner (Li-Cor). Western blots were normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH), and the percent knockout calculated as a fraction of the average of the GRIP1 levels in GFP-infused mice.

Wickens M., Deutschmann A., McGrath A., Parikh V, & Briand L. (2019). Glutamate receptor interacting protein acts within the prefrontal cortex to blunt cocaine seeking.. Neuropharmacology, 157, 107672.

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