SCP2 (Sterol Carrier Protein 2), also known as nonspecific lipid-transfer protein, is a protein involved in intracellular lipid metabolism, particularly in cholesterol transport and steroidogenesis. It facilitates the movement of sterols, fatty acids, and other lipids between cellular membranes, playing a critical role in lipid homeostasis. The SCP2 gene encodes two isoforms: a 13.2 kDa proprotein (SCPx) and a 15.2 kDa mature protein (SCP2), both implicated in peroxisomal and mitochondrial lipid processing.
Antibodies targeting SCP2 are essential tools for studying its expression, localization, and function in various tissues. These antibodies are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to investigate SCP2's role in metabolic pathways, including bile acid synthesis and fatty acid β-oxidation. Dysregulation of SCP2 has been linked to metabolic disorders, such as atherosclerosis, diabetes, and hepatic steatosis, making it a potential biomarker or therapeutic target.
Research utilizing SCP2 antibodies has expanded understanding of its interaction with lipid droplets, peroxisomes, and mitochondria, highlighting its importance in cellular lipid trafficking. Such studies contribute to elucidating mechanisms underlying lipid-related diseases and metabolic syndrome.