Caveolin-1 is a critical structural and regulatory protein of caveolae, small invaginations in the plasma membrane involved in membrane trafficking, signal transduction, and lipid homeostasis. It plays roles in cellular processes such as endocytosis, cholesterol transport, and regulation of endothelial nitric oxide synthase (eNOS). Dysregulation of Caveolin-1 is linked to cancer progression, cardiovascular diseases, and metabolic disorders, making it a key target for biomedical research.
Caveolin-1 antibodies are essential tools for detecting and quantifying this protein in various experimental models. These antibodies, often generated in hosts like rabbits or mice, target specific epitopes within Caveolin-1’s N- or C-terminal domains. Monoclonal antibodies offer high specificity, while polyclonal versions may detect multiple isoforms or post-translationally modified forms, aiding in diverse applications such as Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF).
Validation of Caveolin-1 antibodies is crucial due to potential cross-reactivity with homologous proteins (e.g., Caveolin-2 or -3) or tissue-specific expression variations. Knockout cell lines or siRNA-mediated knockdown are commonly used to confirm specificity. Recent advancements include recombinant antibodies with enhanced reproducibility and phospho-specific antibodies targeting Caveolin-1 phosphorylation sites, which are implicated in disease mechanisms. These tools continue to advance studies on Caveolin-1’s role in membrane dynamics, disease pathways, and therapeutic targeting.