|Detection of Human Perilipin by Western Blot. Western blot shows lysates of human heart (adipose) tissue. PVDF Membrane was probed with 0.25 µg/mL of Human Perilipin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF6615) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). Specific bands were detected for Perilipin at approximately 55-70 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
Perilipin (Perilipin-1/A; also PLIN1 and Lipid droplet-associated protein) is a 62 kDa constitutively phosphorylated protein that belongs to the PAT (Perilipin/Adipophilin/TIP47) family of molecules. Found primarily in mature adipocytes, perilipin-1 interacts with lipid-coat proteins at the edge of the fat droplet and blocks lipase activity. Upon phosphorylation, perilipin-1 becomes a 65-67 kDa molecule that likely promotes the dispersion of docking molecules and provides a scaffold for lipase at the lipid droplet surface. Human perilipin-1 is 522 amino acids (aa) in length. It contains a lipid droplet targeting region (aa 233-364) that contains a polyGlu segment (aa 307-316). Phosphorylation at the N-terminus is necessary for lipase interaction with lipid. One 50-54 kDa human splice variant (perilipin-B) is reported that shows an 85 aa substitution for aa 404-522. This apparently interacts with cell membrane triglycerides. Over aa 8-145, human perilipin-1/A shares 97% aa identity with mouse perilipin-1.