TAGLN (Transgelin), a 22-kDa actin-binding protein belonging to the calponin family, is widely recognized as a marker of smooth muscle differentiation. It plays a critical role in regulating cytoskeletal dynamics, cell motility, and contractile function by stabilizing actin filaments. Initially identified in smooth muscle cells, TAGLN expression is also observed in myofibroblasts and certain cancer-associated fibroblasts. Its involvement in epithelial-mesenchymal transition (EMT) has linked it to pathological processes such as fibrosis, atherosclerosis, and tumor progression.
TAGLN antibodies are essential tools for detecting TAGLN protein expression in research and diagnostics. They are commonly used in techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to study smooth muscle cell phenotypes, vascular remodeling, and cancer metastasis. In cancer biology, elevated TAGLN levels correlate with aggressive tumor behavior and poor prognosis in carcinomas of the breast, colon, and prostate. Conversely, TAGLN downregulation is associated with smooth muscle dysfunction in cardiovascular diseases. Commercial TAGLN antibodies are typically developed against conserved epitopes, ensuring cross-reactivity across human, mouse, and rat samples. Validation includes testing on tissues rich in smooth muscle content (e.g., blood vessels, bladder) and cancer cell lines. Researchers prioritize antibodies with high specificity to avoid cross-reactivity with other calponin family members, ensuring accurate interpretation of TAGLN's role in health and disease.