Anti uqcrc1

Manufactured by Thermo Fisher Scientific

Anti-UQCRC1 is a laboratory reagent used in research applications. It is an antibody that recognizes the UQCRC1 protein, which is a component of the mitochondrial electron transport chain. The core function of Anti-UQCRC1 is to detect and quantify the presence of UQCRC1 in biological samples.

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Lab products found in correlation

Anti ndufa9, by Thermo Fisher Scientific (3 mentions) Polyvinylidene difluoride membrane, by Merck Group (2 mentions) Chemidoc mp station, by Bio-Rad (2 mentions) Halt protease and phosphatase inhibitor cocktail, by Bio-Rad (2 mentions) Luminata immobilon crescendo western hrp substrate, by Merck Group (2 mentions) Sc 393678, by Abcam (2 mentions) Image lab software version 5, by Bio-Rad (2 mentions) Dc protein assay kit, by Bio-Rad (2 mentions) Anti gapdh, by Cell Signaling Technology (2 mentions) Wb blocking reagent, by Roche (2 mentions) Anti ndufb8, by Thermo Fisher Scientific (2 mentions) Anti complex 2 70 kda fp subunit, by Thermo Fisher Scientific (2 mentions) Anti complex 4, by Thermo Fisher Scientific (2 mentions) Anti calnexin, by Merck Group (2 mentions) Anti akt, by Cell Signaling Technology (1 mentions) Anti pakt s473, by Cell Signaling Technology (1 mentions) Anti glp 1r, by Novus Biologicals (1 mentions) Anti glut1, by Merck Group (1 mentions) Anti fgf21, by R&D Systems (1 mentions) Anti sdha, by Thermo Fisher Scientific (1 mentions)

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UQCRC1 (3 citations)

5 protocols using anti uqcrc1

Protein Extraction and Western Blot Analysis

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Protein extracts were isolated from the hearts of 15-day-olds extracted with RIPA lysis buffer (50 mM Tris-HCl at pH 7.4, 150 mM NaCl, 1% Triton X-100, 1% sodium deoxycholate, 0.1% SDS, 1 mM dithiothreitol (DTT), 5 mM EDTA, and Halt Protease and Phosphatase Inhibitor Cocktail from Thermo Fisher Scientific), and the protein concentration was measured using DC Protein Assay kits (Bio-Rad).
Equal quantities of proteins were resolved by SDS-PAGE gels and blotted onto polyvinylidene difluoride membranes (Millipore). Then, the membranes were blocked with 2% bovine serum albumin (BSA) before incubation with the primary and secondary antibodies. The immunoblots were visualized by using Luminata -Immobilon Crescendo Western HRP Substrate (Millipore) on a ChemiDoc MP station (Bio-Rad). Image analysis was performed using Image Lab software version 5.2 (Bio-Rad). The antibodies used for the western blots were as follows: anti-Srsf3 (Abcam, ab198291) anti-Gapdh (Cell Signaling, 2118), anti-Tim50 (Santa-Cruz, sc-393678), anti-Tom20 (Abcam, ab186735), Total OXPHOS antibodies (Abcam, ab110413), and anti-Uqcrc1 (ThermoScientific, PA5-21394).

Dumont A.A., Dumont L., Zhou D., Giguère H., Pileggi C., Harper M.E., Blondin D.P., Scott M.S, & Auger-Messier M. (2021). Cardiomyocyte-specific Srsf3 deletion reveals a mitochondrial regulatory role. FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 35(5).

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Protein Extraction and Western Blot Analysis

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Dumont A., Dumont L., Zhou D., Giguère H., Pileggi C.A., Harper M., Blondin D.P., Scott M.S., & Auger‐Messier M. (2020). Cardiomyocyte-specific Srsf3 deletion reveals a mitochondrial regulatory role.

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Western Blotting Procedure for Protein Analysis

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Western blot analysis was conducted as previously described (Timper et al., 2017 (link)). In brief, membranes were blocked with 10% WB-blocking reagent (Roche, Switzerland) in Tris-buffered saline containing 0.1% Tween-20 (TBS-T), and incubated with primary antibodies, made up in TBS-T (0.1% Tween-20) and 5% Western Blotting-Reagent, at 4°C overnight. The following primary antibodies and dilutions were used: anti-GLP-1R (1:1000, #NBP1-97308, Novus Biologicals), anti-Akt (#4686, Cell Signaling), anti-p-Akt(S473) (#4060, Cell Signaling), anti-NDUFA9 (1:1000, #459100, Invitrogen), anti-NDUFB8 (1:1000, #459210, Invitrogen), anti-Complex II 70 kDa Fp Subunit (1:1000, #459200, Invitrogen), anti-UQCRC1 (1:1000, #459140, Invitrogen), anti-Complex IV (1:1000, #459110, Invitrogen), anti-ATP synthase subunit β (1:1000, #21351, Invitrogen), anti-p-Ser-226-GLUT-1 (#ABN991, Merck Millipore), anti-GLUT-1 (#07-1401, Merck Millipore), anti-FGF21 (#AF3057, R&D Systems) and, as loading control: anti-calnexin (1:4000, #208880, Merck Milipore). Quantification of chemiluminescent signals was performed with the ImageJ (Fiji)-software package (Schneider et al., 2012 (link)).

Timper K., del Río-Martín A., Cremer A.L., Bremser S., Alber J., Giavalisco P., Varela L., Heilinger C., Nolte H., Trifunovic A., Horvath T.L., Kloppenburg P., Backes H, & Brüning J.C. (2020). GLP-1 Receptor Signaling in Astrocytes Regulates Fatty Acid Oxidation, Mitochondrial Integrity, and Function. Cell Metabolism, 31(6), 1189-1205.e13.

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Respiratory Complex Assembly Analysis

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After electrophoresis, gels were further processed for either western blotting or In Gel Activity IGA assays.
In order to analyze the assembly status of respiratory complexes and supercomplexes, proteins separated by BN were transferred onto PVDF membranes and probed with specific antibodies that recognize the different respiratory complexes (anti-NDUFA9, anti-SDHA, anti-Uqcrc1 and anti-COI for complexes I, II, III, IV respectively, all of them from Invitrogen, and anti-β-F₁-ATPase, for complex V, kindly gifted by Dr. J.M. Cuezva). Then, they were incubated with their corresponding secondary antibody, tagged with peroxidase (ThermoFisher Scientific, Waltham, MA, USA). Finally, protein levels were evaluated by immunoblot, using an AmershamTM Imager 600 to document the signal.
Complex I IGA assays were performed after BN-PAGE by incubating the gels at room temperature in the presence of 0.1 M Tris-HCl pH 7.4, 0.14 mM NADH and 1 mg/mL of nitro-blue tetrazolium (NBT) as previously described [80 (link)]. Complex V IGA staining was performed by incubating the gels in 34 mM Tris, 270 mM glycine, 14 mM MgSO₄, 0.2% Pb(NO₃)₂ and 8 mM ATP at pH 7.8, as described before [81 (link)]. After incubation, the gels were photographed with a digital camera using as background a white translucid screen for Complex I and Complex IV and a black screen for Complex V [81 (link)].

Moreno-Loshuertos R., Movilla N., Marco-Brualla J., Soler-Agesta R., Ferreira P., Enríquez J.A, & Fernández-Silva P. (2023). A Mutation in Mouse MT-ATP6 Gene Induces Respiration Defects and Opposed Effects on the Cell Tumorigenic Phenotype. International Journal of Molecular Sciences, 24(2), 1300.

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Western Blot Analysis of Mitochondrial Proteins

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Western blot analysis was conducted as previously described (Timper et al., 2017 (link)). In brief, membranes were blocked with 10% WB-blocking reagent (Roche, Switzerland) in Tris-buffered saline containing 0.1% Tween-20 (TBS-T), and incubated with primary antibodies, made up in TBS-T (0.1% Tween 20) and 5% Western Blotting-Reagent, at 4°C overnight. The following primary antibodies and dilutions were used: anti-AIF (1:1000, #ab32516, Abcam), anti-NDUFA9 (1:1000, #459100, Invitrogen), anti-NDUFB8 (1:1000, #459210, Invitrogen), anti-Complex II 70 kDa Fp Subunit (1:1000, #459200, Invitrogen), anti-UQCRC1 (1:1000, #459140, Invitrogen), anti-Complex IV (1:1000, #459110, Invitrogen), anti-ATP synthase subunit β (1:1000, #21351, Invitrogen) and, as loading control: anti-β-actin (1:2000, #A2228, Sigma Aldrich) or anti-calnexin (1:4000, #208880, Merck Milipore). Quantification of chemiluminescent signals was performed with the ImageJ (Fiji)-software package (Schneider et al., 2012 (link)).

Timper K., Paeger L., Sánchez-Lasheras C., Varela L., Jais A., Nolte H., Vogt M.C., Hausen A.C., Heilinger C., Evers N., Pospisilik J.A., Penninger J.M., Taylor E.B., Horvath T.L., Kloppenburg P, & Brüning J.C. (2018). Mild Impairment of Mitochondrial OXPHOS Promotes Fatty Acid Utilization in POMC Neurons and Improves Glucose Homeostasis in Obesity. Cell reports, 25(2), 383-397.e10.

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