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Thyroid peroxidase (TPO) is a heme-containing enzyme that is essential for the biosynthesis of thyroid hormones.1,2 It exists as a homodimer where each monomer is composed of an extracellular N-terminal signal peptide and propeptide, an ectodomain containing MPO-, CCP-, and EGF-like domains, a transmembrane domain, and an intracellular C-terminal domain.2 TPO is regulated primarily at the transcriptional level by thyroid-stimulating hormone (TSH), which upregulates TPO expression. TPO is expressed by thyroid follicular cells and localizes to the apical plasma membrane in its active state.1,2 It catalyzes the oxidation of iodine, resulting in the formation of monoiodotyrosine (MIT) and diiodotyrosine (DIT) residues on thyroglobulin, a protein that functions as a scaffold for thyroid hormone biosynthesis.3 TPO subsequently catalyzes the oxidative coupling between MIT and DIT residues on thyroglobulin to produce the thyroid hormones triiodothyronine (T3) and thyroxine (T4).3 Serum TPO autoantibodies are a hallmark of autoimmune thyroid diseases, including Hashimoto's disease and Graves' disease, and have been found in patients with breast cancer.4,2 Cayman's TPO (C-Term) Rabbit Monoclonal Antibody (Clone RM368) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.
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1. Structural and functional aspects of thyroid peroxidase. Arch. Biochem. Biophys. 445(2), 269-277 (2006).
2. Thyroid peroxidase as a dual active site enzyme: Focus on biosynthesis, hormonogenesis and thyroid disorders of autoimmunity and cancer. Biochimie 160, 34-45 (2019).
3. The role of thyroglobulin in thyroid hormonogenesis. Nat. Rev. Endocrinol. 15(6), 323-338 (2019).
4. Thyroid autoimmunity: Role of anti-