Detection of Mouse and Rat TRH-degrading Ectoenzyme/|
TRHDE by Western Blot. Western blot shows lysates of SH‑SY5Y human neuroblastoma cell line and embryonic rat brain hippocampal glial. PVDF membrane was probed with 1 µg/mL of Goat Anti-Mouse/Rat TRH-degrading Ectoenzyme/TRHDE Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2985) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for TRH-degrading Ectoenzyme/TRHDE at approximately 125 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.
TRHDE, also known as pyroglutamyl peptidase II and thyroliberinase, is a metalloprotease that specifically removes pyroglutamate from thyrotropin-releasing hormone, a tripeptide of L-pyroglutamyl-L-histidyl-L-prolineamide. TRH functions as a hypothalamic hypophysiotropic neuropeptide and neurotransmitter/neuromodulator within the central nervous system (1). Inhibitors of TRHDE have potential applications as research and therapeutic agents because TRHDE inactivates TRH (2). TRHDE is a type II transmembrane protein and a soluble form is also present in the serum (1). The recombinant mouse TRHDE corresponds to the ectodomain of the enzyme. Its amino acid sequence is 97% and 95% identical to that of rat and human.
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