Anti ndufb8

Manufactured by Abcam

Sourced in United States, United Kingdom

Anti-NDUFB8 is a laboratory equipment product used for research purposes. It is an antibody that specifically binds to NDUFB8, a subunit of the NADH:Ubiquinone Oxidoreductase (Complex I) of the mitochondrial respiratory chain. This antibody can be used for the detection and analysis of NDUFB8 in various experimental settings.

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NDUFB8 (19 citations) Mouse anti-NDUFB8 (2 citations)

3 protocols using anti ndufb8

Protein Profiling of Liver and Mitochondrial Lysates

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The liver lysate and mitochondrial lysate proteins were separated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. These proteins were then transferred to polyvinylidene difluoride membranes (Millipore, Bedford, MA, USA) and blocked overnight at 4°C with 1–3% skim milk and 0.1% Tween 20 in Tris-buffered saline, which was followed by incubation at room temperature for 1 h with a primary antibody. Anti-rabbit carnitine palmitoyl transferase I (CPT I), anti-rabbit CPT II (Alpha Diagnostic International, San Antonio, TX, USA), anti-rabbit SREBP1 (Santa Cruz Biotechnology Inc., Santa Cruz, CA, USA), or anti-bacterially expressed mouse CCAAT/enhancer-binding protein homology protein (CHOP) fusion protein (Abcam, Cambridge, England) were used for the liver lysate proteins. Anti-SOD2 (Abcam), anti-Grp75 (mitochondrial heat shock protein70; Abcam), or anti-NDUFB8 (mitochondrial complex I) antibody (Abcam) were used for the mitochondrial lysates. The proteins were blocked for 1 h at room temperature and then incubated overnight at 4°C with a Phospho-stat3 (pSTAT3) antibody (Cell Signaling Technology Inc., Danvers, MA, USA) and a Phospho-Smad1/Smad5/Smad8 (pSMAD1/5/8) antibody (Cell Signaling Technology Inc.).The anti-acetylhistoneH3K9 and anti-histoneH3 (Cell Signaling Technology Inc,) were used for the nuclear lysates.

Korenaga M., Nishina S., Korenaga K., Tomiyama Y., Yoshioka N., Hara Y., Sasaki Y., Shimonaka Y, & Hino K. (2014). Branched-chain amino acids reduce hepatic iron accumulation and oxidative stress in hepatitis C virus polyprotein-expressing mice. Liver International, 35(4), 1303-1314.

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Western Blot Analysis of Cellular Proteins

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Cells were washed twice with ice-cold PBS at the indicated time and lysed in lysing buffer (5 g SDS, 0.37 g EDTA, 0.2922 g NaCl, 1 mL 1M Tris-Cl, adjust pH to 7.5 with HCl and add ddH₂O to 100 mL). The concentration of proteins was quantified using a BCA (bicinchoninic acid) protein assay (Thermo Fisher, Rockford, IL, USA). Protein samples were run on a standard SDS-PAGE and transferred to PVDF membranes, which were then saturated with 5% non-fat milk. Subsequently, the membranes were blotted with specific primary antibodies overnight at 4 °C. The primary antibodies used in this study were: anti-ATP5A (Cat#ab14748), anti-NDUFB8 (Cat#ab110242), and anti-FASN (Cat#ab128870) antibodies were purchased from ABCAm (Cambridge, MA, USA). Anti-Vinculin (Cat#13901) antibody was purchased from Cell Signaling Technology (Cambridge, MA, USA). Then, the membranes were incubated with appropriate horseradish peroxidase-conjugated secondary antibodies, and the bands were visualized by chemiluminescence using an imaging system (Bio-Rad Laboratories, Carlsbad, CA, USA).

Zhang M., Xiang R., Glorieux C, & Huang P. (2022). PLA2G2A Phospholipase Promotes Fatty Acid Synthesis and Energy Metabolism in Pancreatic Cancer Cells with K-ras Mutation. International Journal of Molecular Sciences, 23(19), 11721.

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Western Blot Analysis of Metabolic and Immune Markers

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Cells were collected and lysed with NP40 Lysis Buffer (Beyotime) with 1 mM Phenylmethanesulfonyl fluoride (Beyotime). Each quantity of 10⁶ cells was lysed with 50 μL NP40 buffer. The cell lysates were collected by centrifugation at 13,000 rpm at 4°C for 10 minutes. Protein loading buffer (Beyotime) was added, and the samples boiled at 95°C for 10 minutes. The isolated protein was subjected to SDS-PAGE on 4% to 20% polyacrylamide gels (ACE Biotechnology, Nanjing, China) and transferred to NC membranes (Millipore, St. Louis, MO, USA). The membranes were incubated with a primary antibody and secondary antibody. The primary antibodies included anti-Glut1, anti-LDHA, anti-NRF1, anti-NRF2, anti-GZMB, anti-Actin (Beyotime), anti-SIRT1 (Abclonal, Wuhan, China), anti-HK2, anti-CPT1α, anti-PGC1, anti-MTCO2, anti-TFAM, anti-GZMA, anti-GZMK, anti-PRF1, anti-PD-1, anti-TIM-3, anti-CTLA-4, anti-NDUFB8, anti-SDHB, anti-MTCO1, anti-UQCRC2, and anti-ATP5A (Abcam, Cambridge, UK). The secondary antibodies included HRP-labeled goat anti-rabbit and HRP-labeled goat anti-mouse antibodies (Beyotime). Finally, the proteins were detected by West Femto Maximum Sensitivity Substrate (ThermoFisher).

Liu Y., An L., Yang C., Wang X., Huang R, & Zhang X. (2023). Ginsenoside Rg1 improves anti-tumor efficacy of adoptive cell therapy by enhancing T cell effector functions. Blood Science, 5(3), 170-179.

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