Recombinant Human PLIN1 protein

Perilipin 1 (PLIN1) is a lipid droplet-associated protein critical for regulating lipid storage and metabolism in adipocytes. As a member of the perilipin family, it coats the surface of lipid droplets, acting as a protective barrier and dynamic regulator of lipolysis. PLIN1 modulates the access of lipases, such as hormone-sensitive lipase (HSL) and adipose triglyceride lipase (ATGL), to stored triglycerides. During fasting or β-adrenergic stimulation, phosphorylation of PLIN1 by protein kinase A (PKA) triggers conformational changes, facilitating lipase recruitment and lipid mobilization. Conversely, in the unphosphorylated state, PLIN1 stabilizes lipid droplets by inhibiting basal lipolysis.

Recombinant PLIN1 proteins are engineered to study its structure-function relationships and interactions with metabolic enzymes. Typically produced in bacterial or mammalian expression systems, these proteins retain key domains, including the N-terminal PAT domain (shared by perilipin, ADRP, and TIP47) and C-terminal lipid-binding regions. Researchers utilize recombinant PLIN1 to investigate lipid droplet biogenesis, obesity-related metabolic disorders, and insulin resistance. Mutagenesis studies have identified residues critical for phosphorylation-dependent lipolytic regulation, while structural analyses reveal insights into its amphipathic helices that anchor to lipid droplets.

Applications extend to drug discovery, particularly for targeting dysregulated lipid metabolism in conditions like diabetes and atherosclerosis. Recombinant PLIN1 also serves as a tool to explore crosstalk between lipid storage organelles and other cellular pathways, including autophagy and inflammation. Its role in cancer cell energetics and steatosis in non-adipose tissues further underscores its biomedical relevance. By enabling precise biochemical and cell-based assays, recombinant PLIN1 continues to advance our understanding of lipid homeostasis and metabolic disease mechanisms.