The UQCR10 antibody is a research tool designed to detect and quantify Ubiquinol-cytochrome c reductase complex subunit 10 (UQCR10), a key component of mitochondrial Complex III (cytochrome bc₁ complex) in the electron transport chain. Complex III plays a critical role in oxidative phosphorylation by catalyzing electron transfer from ubiquinol to cytochrome c, coupled with proton pumping across the mitochondrial inner membrane to generate ATP. UQCR10. encoded by the UQCR10 gene, is a nuclear DNA-encoded structural subunit that contributes to the assembly and stability of Complex III.
Antibodies targeting UQCR10 are widely used in studies exploring mitochondrial function, cellular energy metabolism, and diseases linked to oxidative phosphorylation defects, such as cancer, neurodegenerative disorders, and metabolic syndromes. These antibodies enable techniques like Western blotting, immunofluorescence, and immunohistochemistry to assess UQCR10 expression levels, subcellular localization, and interactions with other Complex III subunits (e.g., cytochrome b, c1).
Research using UQCR10 antibodies has revealed its potential role in modulating reactive oxygen species (ROS) production and apoptosis. Dysregulation of UQCR10 expression has been associated with tumor progression and chemoresistance, making it a biomarker of interest in oncology. Validation of UQCR10 antibodies typically includes testing in knockdown models or tissues with known expression patterns to confirm specificity. Commercial UQCR10 antibodies are often raised in rabbits or mice using peptide antigens derived from conserved regions of the protein, with reactivity confirmed across human, mouse, and rat samples.