Recombinant Human NT5E protein

NT5E (Ecto-5'-nucleotidase), also known as CD73. is a membrane-bound glycoprotein enzyme encoded by the NT5E gene. It plays a critical role in purinergic signaling by catalyzing the hydrolysis of extracellular adenosine monophosphate (AMP) to adenosine, a potent signaling molecule. This enzymatic activity links NT5E to the regulation of immune responses, inflammation, and tissue homeostasis. Adenosine binds to specific receptors (A1. A2A, A2B, A3) on immune and stromal cells, modulating pathways that can suppress immune activation—a mechanism exploited by tumors to evade immune surveillance.

Recombinant NT5E protein is produced through genetic engineering, typically using mammalian expression systems to ensure proper post-translational modifications. The recombinant form often retains the extracellular domain (residues 1-549) while omitting the transmembrane and cytoplasmic regions, creating a soluble protein for experimental applications. It is widely used in vitro to study adenosine-mediated processes, including tumor immune evasion, angiogenesis, and fibrosis. Researchers utilize recombinant NT5E to investigate its interaction with therapeutic antibodies or inhibitors targeting its enzymatic active site.

Clinically, NT5E overexpression correlates with poor prognosis in cancers like melanoma, glioblastoma, and breast cancer, making it a potential biomarker and therapeutic target. Its role in immune suppression has spurred development of anti-CD73 antibodies for combination therapies with immune checkpoint inhibitors. Beyond oncology, NT5E dysfunction is implicated in cardiovascular diseases and autoimmune disorders. Recombinant protein studies continue to clarify its structural nuances, including dimerization requirements and zinc-binding catalytic sites, driving innovations in precision medicine approaches.