Mops sds running buffer

Manufactured by Merck Group

MOPS SDS Running Buffer is a laboratory buffer solution used for the electrophoretic separation of proteins in polyacrylamide gel electrophoresis (PAGE) applications. It provides a consistent pH environment and ionic strength to facilitate the migration of proteins during the electrophoresis process.

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Lab products found in correlation

P7170, by Merck Group (2 mentions) Immobilon crescendo western hrp substrate, by Thermo Fisher Scientific (2 mentions) Bicinchoninic acid assay, by Thermo Fisher Scientific (1 mentions) Amersham imager ai680, by GE Healthcare (1 mentions) Lds sample buffer 4x, by Thermo Fisher Scientific (1 mentions) Ge amersham imager ai680, by GE Healthcare (1 mentions) Nupage bis tris sds page, by Thermo Fisher Scientific (1 mentions) Ipvh00010, by Merck Group (1 mentions)

Close spelling variants of this product

MOPS buffer (18 citations) TruPAGE Tris-MOPS SDS Express Running Buffer (3 citations) SDS) running buffer (2 citations)

2 protocols using mops sds running buffer

Isolation and Characterization of Extracellular Fraction

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EF was isolated from quadriceps of wildtype mice using the indicated centrifugation speeds. EF volume was measured, and protein concentration was determined using bicinchoninic acid assay (Fisher Scientific, 23,225). Samples were denatured in LDS sample buffer (4X) (Invitrogen, NP0007) for 5 min at 95 °C. 10 μg of protein was resolved on a 4–12% NuPAGE BisTris SDS–PAGE (Invitrogen) with MOPS SDS Running Buffer (Sigma Aldrich, M1254), transferred to a polyvinylidene difluoride (PVDF) membrane (Millipore, IPVH00010) using transfer buffer (25 mM Tris, 192 mM glycine, 20% (v/v) methanol). To control for correct loading and transfer, Ponceau staining was performed according to manufacturer's instructions (Sigma Aldrich, P7170). Membranes were blocked in 5% BSA or 5% milk in TBS containing 0.05% Tween-20 (TBST) and incubated overnight at 4 °C with primary antibody. Secondary HRP-conjugated antibodies were used, membranes were incubated in Immobilon Crescendo Western HRP substrate (Fisher Scientific, WBLUR0500), and imaged (GE Amersham Imager AI680). The following antibodies were used: Mouse Monoclonal Anti-OXPHOS cocktail, Abcam Cat#: ab110413; RRID: AB_2629281; Rabbit Monoclonal Anti-GOLGIN 97, Cell signaling Cat#: 13,192; RRID: AB_2798144; Rabbit Monoclonal Anti-LAMIN A/C, Abcam Cat#: ab169532.

Ducommun S., Jannig P.R., Cervenka I., Murgia M., Mittenbühler M.J., Chernogubova E., Dias J.M., Jude B., Correia J.C., Van Vranken J.G., Ocana-Santero G., Porsmyr-Palmertz M., McCann Haworth S., Martínez-Redondo V., Liu Z., Carlström M., Mann M., Lanner J.T., Teixeira A.I., Maegdefessel L., Spiegelman B.M, & Ruas J.L. (2024). Mustn1 is a smooth muscle cell-secreted microprotein that modulates skeletal muscle extracellular matrix composition. Molecular Metabolism, 82, 101912.

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Protein Denaturation and Western Blotting

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Samples were denatured in SDS sample buffer (6X) (0.375 M Tris pH 6.8, 12 % SDS, 60 % glycerol, 0.6 M DTT, 0.06 % bromophenol blue) for 5 min at 95 °C. 10–20 μg of protein was resolved on a 4–12% NuPAGE BisTris SDS–PAGE (Invitrogen) with MOPS SDS Running Buffer (Sigma Aldrich, M1254).
SDS-PAGE used for silver staining (Life Technologies, 24612) were processed according to the manufactures protocol, respectively.
For western blot, SDS-PAGE was transferred to a polyvinylidene difluoride (PVDF) membrane (Millipore, IPVH00010) using Towbin transfer buffer (25 mM Tris, 192 mM glycine, 20% (v/v) methanol). To control for correct loading and transfer, Ponceau staining was performed according to manufactures instructions (Sigma Aldrich, P7170). Membranes were blocked in 5% BSA or 5% milk in TBS containing 0.05% Tween (TBST) and incubated overnight at 4 °C with primary antibody. Secondary HRP-conjugated antibodies were used, membranes were incubated in Immobilon Crescendo Western HRP substrate (Fisher Scientific, WBLUR0500), and imaged (GE Amersham Imager AI680). Used antibodies are displayed in the key resource table.

Mittenbühler M.J., Jedrychowski M.P., van Vranken J.G., Sprenger H.G., Wilensky S., Dumesic P.A., Sun Y., Tartaglia A., Bogoslavski D., A M., Xiao H., Blackmore K.A., Reddy A., Gygi S.P., Chouchani E.T, & Spiegelman B.M. (2023). Isolation of extracellular fluids reveals novel secreted bioactive proteins from muscle and fat tissues. Cell metabolism, 35(3), 535-549.e7.

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