Paxillin (PXN) is a multifunctional adaptor protein primarily involved in cell adhesion, migration, and signaling. Discovered in the early 1990s, it localizes to focal adhesions, dynamic structures that mediate interactions between the extracellular matrix (ECM) and the actin cytoskeleton. PXN serves as a scaffold, integrating signals from integrins, growth factor receptors, and cytoskeletal regulators. Its structure includes LD motifs and LIM domains, which facilitate binding to kinases (e.g., FAK, Src), phosphatases, and other adhesion-related proteins, enabling coordination of cell motility and survival pathways. Dysregulation of PXN expression or phosphorylation is linked to cancer metastasis, fibrosis, and cardiovascular diseases, making it a biomarker for pathological processes. PXN antibodies are essential tools for studying these mechanisms. They are widely used in techniques like Western blotting, immunofluorescence, and immunohistochemistry to assess PXN expression, post-translational modifications (e.g., tyrosine phosphorylation at Y31/Y118), and subcellular localization. Commercial PXN antibodies vary in specificity (e.g., targeting N-terminal vs. C-terminal regions) and applications, requiring validation for experimental contexts. Recent research explores PXN's role in mechanotransduction and its potential as a therapeutic target in invasive cancers, driving demand for high-quality, well-characterized antibodies.