|Detection of Human Renalase by Western Blot. Western blot shows lysates of human plasma. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human Renalase Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5350) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for Renalase at approximately 37 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.|
Renalase is a novel, 35‑37 kDa FAD-dependent amine oxidase that is secreted primarily by glomerular and renal tubule epithelium. It presumably degrades catecholamines and lowers blood pressure by decreasing heart rate and cardiac contractility. In addition to renal cells, Renalase is produced by skeletal and cardiac muscle fibers. The human Renalase precursor is 342 amino acids (aa) in length. It contains an FAD binding domain (aa 4‑35) that overlaps a signal sequence (aa 1‑17), followed by an amine oxidase segment (aa 75‑339). Renalase circulates as both a monomer (from kidney) and homodimer (from heart). There is one potential splice variant that shows a 22 aa substitution for aa 294‑342. Over aa 2‑342, human Renalase shows 72% aa identity to mouse Renalase.
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