Uncoupling protein (UCP1) is a 32 kDa, mitochondrial inner membrane protein. It is active as a proton channel forming dimer. It can bind purine nucleotides and is capable of being stimulated by fatty acids.
Anti-UCP-1 specifically recognizes human, mouse and rat UCP-1. Staining of the UCP-1 band is specifically inhibited with the immunizing peptide. The epitopes recognized are compatible with routine formalin-fixation and paraffin-embedding.
synthetic peptide corresponding to human UCP1 sequence (amino acids 145-159) with N-terminal cysteine added, conjugated to KLH. The corresponding sequence is identical in rat and mouse UCP1.
Anti-UCP-1 antibody produced in rabbit has been used in western blotting and immunohistochemistry.
Uncoupling proteins (UCPs) are transporters functioning as enzymatic uncouplers of oxidative phosphorylation. They can return protons pumped by the respiratory chain to the mitochondrial matrix. UCP-1 is exclusively expressed in brown adipose tissue (BAT) in rodents and in neonates where it is regulated by norepinephrine and thyroid hormones. UCP-1 has been shown to depend on CoQ (ubiquinone) as an obligatory co-factor.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.
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