Phosphos-Adipose Triglyceride Lipase (Ser406) Rabbit Polyclonal Antibody

Adipose Triglyceride Lipase (ATGL), also known as PNPLA2, is the rate-limiting enzyme that catalyzes the first step of triglyceride hydrolysis, converting triacylglycerols into diacylglycerols and free fatty acids. It is a member of the patatin-like phospholipase domain-containing protein family and contains a conserved N-terminal patatin domain (approximately spanning amino acids 10–178) that harbors a catalytic dyad consisting of Ser47 and Asp166. ATGL is highly expressed in white and brown adipose tissue but is also present at lower levels in most other tissues, where it plays important roles in cellular lipid mobilization. Its enzymatic activity is tightly regulated by protein-protein interactions: it is co-activated by Comparative Gene Identification-58 (CGI-58) and inhibited by G0/G1 Switch Gene 2 (G0S2). Mutations in the ATGL gene cause Neutral Lipid Storage Disease with Myopathy (NLSDM), characterized by triglyceride accumulation in multiple tissues and severe skeletal and cardiac myopathy. While hormone-sensitive lipase (HSL) was traditionally considered the key lipolytic enzyme, ATGL is now recognized as essential for maintaining basal lipolytic activity, whereas HSL is more responsive to stimulated lipolysis.