Human Atrial Natriuretic Peptide/ANP Antibody

ANP (Atril Natriuetic Peptide; also known as gamma -ANP, CDP/cardiodilatin-related peptide and CDD-ANF) is a secreted member of the natriuretic peptide family of molecules. It is expressed in multiple cell types, including atrial myocardiocytes, macrophages and select hypothalamic neurons. The C-terminus of ANP (or ANF) is reported to have a wide range of activities. It is best known to promote sodium and water excretion, but is also known to inhibit aldosterone and vasopressin secretion, while promoting testosterone and LH release. Human (pro)ANP is synthesized as a 153 amino acid (aa) preproprecursor that contains a 25 aa signal sequence, cardiodilatin-related peptide (aa 26-55), a prosequence (aa 56-123) and a C-terminal atrial natriuretic factor motif (aa 124-151) that may or may not be accompanied by a dibasic Arg fragment. Although multiple enzymes are reported to be active on proANP, transmembrane Corin would appear to be central to normal extracellular proteolytic processing and the generation of ANP. Notably, and depending upon the tissue, proANP can also be cleaved at alternate sites, including Ala120 and Arg126. There is at least one isoform variant that contains a 12 aa addition to the C-terminus of the proprecursor, resulting in an ANP that is 40 aa in length. Over aa 26-151 (proANP), human proANP shares 84% aa sequence identity with mouse proANP.