Function
Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. Exhibits a strong preference for the hydrolysis of long-chain fatty acid esters at the sn-2 position of the glycerol backbone and acts coordinately with LIPE/HLS and DGAT2 within the lipolytic cascade. Also possesses acylglycerol transacylase and phospholipase A2 activities.
Biological Context
Subcellular Location: Lipid droplet; Cell membrane (Multi-pass membrane protein); Cytoplasm
Tissue Specificity: Highest expression in adipose tissue. Also detected in heart, skeletal muscle, and portions of the gastrointestinal tract. Detected in normal retina and retinoblastoma cells. Detected in retinal pigment epithelium and, at lower intensity, in the inner segments of photoreceptors and in the ganglion cell layer of the neural retina (at protein level)
Disease Association: [Genetic variations in PNPLA2 may be associated with risk of diabetes mellitus type 2] | Neutral lipid storage disease with myopathy (NLSDM) : Neutral lipid storage disorder (NLSD) with myopathy but without ichthyosis. NLSDs are characterized by the presence of triglyceride-containing cytoplasmic droplets in leukocytes and in other tissues, including bone marrow, skin, and muscle. Individuals with NLSDM did not show obesity, in spite of a defect in triglyceride degradation in fibroblasts and in marked triglyceride storage in liver, muscles, and other visceral cells. [The disease is caused by variants affecting the gene represented in this entry]
Pathway: Glycerolipid metabolism; triacylglycerol degradation
Product Specifications
Recombinant Human Patatin-like phospholipase domain-containing protein 2 (PNPLA2) is a recombinant protein from Homo sapiens (Human), expressed in E.coli, covering amino acids 1-504aa, with N-terminal 6xHis-SUMO-tagged tag, molecular weight 71.3kDa, purity Greater than 90% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications.
