ADAM12 (A Disintegrin and Metalloprotease 12) is a member of the ADAM family of transmembrane and secreted proteins, which play critical roles in cell adhesion, proteolysis, and cell signaling. ADAM12 exists in two splice variants: the membrane-anchored ADAM12-L (long form) and the secreted ADAM12-S (short form). Both isoforms share a conserved structure, including a prodomain, metalloprotease, disintegrin, cysteine-rich, and EGF-like domains, but differ in their C-terminal regions. ADAM12 is implicated in extracellular matrix remodeling, cell-cell interactions, and growth factor shedding, with essential functions in embryonic development, tissue repair, and cancer progression.
ADAM12 is highly expressed during embryogenesis, particularly in musculoskeletal and cardiovascular systems, but its expression is low in most adult tissues. Aberrant upregulation of ADAM12 has been linked to pathological conditions, including fibrosis, cardiovascular diseases, and various cancers (e.g., breast, lung, and gastric cancers), where it promotes tumor growth, invasion, and metastasis by modulating pathways like TGF-β and EGFR. Its role in cleaving insulin-like growth factor binding proteins (IGFBPs) also highlights its involvement in regulating cell proliferation.
Antibodies targeting ADAM12 are vital tools for studying its expression, localization, and function. They are used in techniques such as Western blotting, immunohistochemistry, and immunofluorescence to investigate ADAM12's role in disease mechanisms or developmental processes. Some studies explore ADAM12 antibodies for diagnostic or therapeutic applications, given its association with aggressive cancer phenotypes and fibrotic disorders. However, challenges remain in ensuring antibody specificity and optimizing their use in clinical settings. Research continues to elucidate ADAM12's complex roles and therapeutic potential.