Detection of Human, Mouse, and Rat NGF R/TNFRSF16 by Western Blot.Western blot shows lysates of human colon cancer tissue, NIH‑3T3 mouse embryonic fibroblast cell line, PC‑12 rat adrenal pheochromocytoma cell line, HeLa human cervical epithelial carcinoma cell line, and HEK293T human embryonic kidney cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/Mouse/Rat NGF R/TNFRSF16 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF367) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for NGF R/TNFRSF16 at approximately 45 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
p75 neurotrophin receptor, also named low affinity NGF receptor (NGF R), is a type I transmembrane protein that belongs to the tumor necrosis factor receptor family. NGF R cDNA encodes a 427 amino acid (aa) residue precursor protein with a 28 aa residue signal peptide, a 222 aa residue extracellular domain, a 22 aa residue transmembrane domain and a 155 aa residue intracellular domain. The extracellular region contains four cysteine-rich domains and binds NGF, BDNF, NT-3, and NT-4 approximately equally with low affinity. The cytoplasmic region contains a subtype 2 death domain.
NGF R expression has been shown to occur widely during development and in the adult. Expression has been detected in both neuronal and non-neuronal cells. NGF R was originally reported to function as a positive regulator of TrkA activity. NGF R has also been shown to signal by itself. Depending on its cellular environment, NGF R has now been shown to regulate cell migration, gene expression and to mediate apoptosis. Recombinant NGF R Fc chimera binds NGF with high affinity and is a potent NGF antagonist. Naturally occurring truncated NGF R containing the extracellular domain and lacking the transmembrane or intracellular domain has been detected in vivo in urine, plasma and in amniotic fluid of humans and rats.
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