|Detection of Human and Mouse Lipoprotein Lipase/LPL by Western Blot. Western blot shows lysates of SH‑SY5Y human neuroblastoma cell line and NMuMG mouse mammary gland epithelial cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human Lipoprotein Lipase/LPL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7197) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for Lipoprotein Lipase/LPL at approximately 56 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|Lipoprotein Lipase/LPL in SH‑SY5Y Human Cell Line. Lipoprotein Lipase/LPL was detected in immersion fixed SH‑SY5Y human neuroblastoma cell line using Goat Anti-Human Lipoprotein Lipase/LPL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7197) at 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Goat IgG Secondary Antibody (red, upper panel; Catalog # NL001) and counterstained with DAPI (blue, lower panel). Specific staining was localized to cell surfaces and cytoplasm. View our protocol for Fluorescent ICC Staining of Cells on Coverslips. This application has not been tested in mouse samples.|
LPL (LipoProtein Lipase; also LIPD) is a 53-56 kDa glycoprotein member of the Lipase family, AB Hydrolase superfamily of molecules. It is produced by multiple cell types, including adipocytes, skelelal muscle cells and macrophages. Once secreted, the circulating enzyme ultimately becomes immobilized on the surface of endothelium by binding to cell surface heparan sulfate. Here, it hydrolyzes triglycerides embedded in chylomicrons and VLDLs by homodimerizing and interacting with apoC2. Mature human LPL is 448 amino acids (aa) in length. It contains an enzymatic region (aa 37-334) plus one protein-interaction PLAT domain (aa 341-465). Over aa 28-154, human LPL shares 91% aa identity with mouse LPL.
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