|Adrenomedullin/ADM in Human Heart. Adrenomedullin/ADM was detected in immersion fixed paraffin-embedded sections of human heart using Goat Anti-Human Adrenomedullin/ADM Antigen Affinity-purified Polyclonal Antibody (Catalog # AF6108) at 10 µg/mL overnight at 4 °C. Before incubation with the primary antibody tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (Catalog # CTS013). Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
Adrenomedullin (ADM; also AM) is a secreted, monomeric, 6 kDa member of the Adrenomedullin family of molecules. It is widely expressed, being found in smooth muscle cells, endothelium, adrenal medulla chromaffin cells, fibroblasts and keratinocytes. ADM has multiple functions, including vasodilation, the maintenance of vascular integrity, and the suppression of inflammatory mediator secretion. The human ADM preproprecursor is 185 amino acids (aa) in length. It contains a 21 aa signal sequence, a processed 20 aa peptide termed PAMP (aa 22-41), an N-terminal propeptide (aa 45-92), the ADM precursor (amidation is required for maturation) (aa 95‑147), and a C-terminal propeptide (aa 148-185). The ADM precursor with a terminal Gly147 circulates naturally with bioactive, mature amidated ADM (aa 95‑146). Depending upon the tissue, truncated forms of ADM likely also occur, including variants spanning aa 120-146 and 128-146. Over aa 22-147, the human ADM proprecursor shares 70% aa identity with mouse ADM proprecursor.