SERPINB8. a member of the serine protease inhibitor (serpin) superfamily, plays a regulatory role in diverse cellular processes by inhibiting specific proteases. It is primarily known for its involvement in skin barrier maintenance, neuroprotection, and cancer progression. SERPINB8 inhibits enzymes like furin and cathepsin L, modulating proteolytic cascades critical for cellular homeostasis, differentiation, and apoptosis. Dysregulation of SERPINB8 has been linked to skin disorders (e.g., psoriasis), neurodegenerative diseases, and tumor metastasis, highlighting its pathophysiological relevance.
SERPINB8 antibodies are essential tools for studying its expression, localization, and function. These antibodies are commonly used in techniques such as Western blotting, immunohistochemistry (IHC), and immunofluorescence to detect SERPINB8 in human, mouse, or rat tissues. They often target conserved epitopes within the reactive center loop (RCL), a key region mediating protease interaction. High-quality SERPINB8 antibodies enable researchers to explore its role in disease mechanisms, evaluate its diagnostic potential, or validate interactions with proteases in experimental models. Validation via knockout controls or peptide blocking ensures specificity, supporting reliable data in both basic research and clinical applications.