ATGL Recombinant Rabbit mAb

ATGL is the rate-limiting enzyme that initiates the hydrolysis of triglycerides in living organisms. This protein consists of 504 amino acids and contains a conserved patatin domain as its core functional region, which harbors the Ser-Asp catalytic dyad (Ser47 and Asp166) responsible for catalyzing the first step of triglyceride hydrolysis. ATGL is expressed in various tissues including white adipose tissue, brown adipose tissue, heart, liver, and small intestine, where it plays a central role in maintaining whole-body energy homeostasis by hydrolyzing triglycerides into diglycerides and free fatty acids. The function of ATGL is tightly regulated: its catalytic activity requires binding to the cofactor CGI-58 for full activation, while inhibitors such as G0S2, CIDEC, and members of the PLIN family can suppress its activity through direct interaction. Dysfunction of ATGL leads to severe metabolic disorders; mutations in its gene can cause neutral lipid storage disease (NLSD) characterized by triglyceride accumulation in multiple tissues, while systemic ATGL-deficient mice exhibit severe phenotypes including cardiomyopathy and premature death. In recent years, research has also revealed novel functions of ATGL, such as its ability to hydrolyze bacterial endotoxin lipopolysaccharide (LPS), thereby negatively regulating non-canonical inflammasome activation, offering potential new therapeutic targets for inflammatory diseases like sepsis.