Recombinant Human ATP5F1B protein

ATP5F1B, also known as ATP synthase subunit beta or ATP5B, is a critical component of the mitochondrial ATP synthase complex (Complex V), which plays a central role in cellular energy production. This enzyme catalyzes the synthesis of ATP from ADP and inorganic phosphate during oxidative phosphorylation, utilizing the proton gradient generated across the inner mitochondrial membrane. The ATP5F1B gene, located on chromosome 12q13.3 in humans, encodes the β-subunit of the F1 catalytic core of ATP synthase. As one of the core subunits, it participates in the conformational changes required for ATP synthesis and hydrolysis, making it indispensable for mitochondrial function.

Recombinant ATP5F1B protein is produced through genetic engineering techniques, typically by expressing the cloned gene in heterologous systems like *E. coli* or mammalian cell cultures. This allows large-scale production of the purified protein for functional and structural studies. The recombinant form retains the enzymatic activity of native ATP5F1B, enabling researchers to investigate its role in ATP synthesis, mitochondrial dynamics, and cellular metabolism under controlled conditions. Its structural features, including nucleotide-binding domains and interaction interfaces with other subunits, are often analyzed to understand mechanistic details or mutations linked to diseases.

Studies involving recombinant ATP5F1B have contributed to insights into mitochondrial disorders, neurodegenerative diseases, and cancer, where dysregulation of ATP synthase is implicated. It also serves as a tool for drug screening, antibody development, and exploring metabolic adaptations in hypoxia or stress. Additionally, its interactions with regulatory proteins or inhibitors (e.g., oligomycin) are frequently probed to identify therapeutic targets. Overall, recombinant ATP5F1B is a vital reagent for dissecting mitochondrial bioenergetics and its pathophysiological connections.