The S100A12 antibody is a crucial tool for studying the S100A12 protein, a member of the S100 calcium-binding protein family. S100A12. also known as calgranulin C or EN-RAGE, is encoded by the S100A12 gene and primarily expressed in granulocytes, monocytes, and certain epithelial cells. It functions as a damage-associated molecular pattern (DAMP) molecule, playing roles in inflammation, immune response, and cell differentiation by binding to calcium and interacting with receptors like the receptor for advanced glycation end products (RAGE). Dysregulated S100A12 expression is linked to chronic inflammatory diseases (e.g., inflammatory bowel disease, rheumatoid arthritis), infections, and cancers, making it a biomarker for disease activity and therapeutic targeting.
S100A12 antibodies are designed to detect and quantify this protein in research and diagnostic settings. They are widely used in techniques such as Western blotting, immunohistochemistry (IHC), and enzyme-linked immunosorbent assays (ELISA) to study S100A12's expression patterns, cellular localization, and involvement in pathological processes. Monoclonal antibodies offer high specificity, while polyclonal antibodies may detect multiple epitopes, enhancing sensitivity. Commercially available S100A12 antibodies aid in elucidating its role in inflammation-mediated tissue damage and its potential as a therapeutic target. Inhibiting S100A12-RAGE signaling, for instance, has shown promise in reducing inflammatory responses in preclinical models. These antibodies also support clinical research, enabling the correlation of S100A12 levels with disease severity, thereby guiding diagnosis and treatment strategies.