UCP1 antibody

Mitochondrial oxidative phosphorylation makes possible ATP synthesis using the energy available from substrate oxidation at the respiratory chain. These processes are coupled through the proton electrochemical potential gradient generated during the transfer of electrons from the substrate to oxygen. The uncoupling proteins (UCPs) are mitochondrial inner membrane proteins that are considered to be transporters functioning as enzymatic uncouplers of oxidative phosphorylation. They are capable of returning protons pumped by the respiratory chain to the mitochondrial matrix. Uncoupling proteins currently comprise UCP1, UCP2, UCP3, UCP4, and UCP5. UCP1 is a 32 kDa protein that is active as a proton channelforming dimer. It can bind purine nucleotides and is capable of being stimulated by fatty acids. Proton transport by UCP1 has been shown to depend on CoQ (ubiquinone) as an obligatory cofactor. UCP1 is exclusively expressed in BAT in rodents and in neonates where it is regulated by norepinephrine and thyroid hormones. Stimulated BAT is able to dissipate energy as heat via uncoupled mitochondrial respiration. The liberated heat can serve several physiological functions, e.g. for body heating during emergence from hibernation or during cold exposure, for burning body fat and consequently for body weight regulation.