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Description
Purified anti-LRP2. Megalin or low density lipoprotein-related protein 2 (LRP2), is a multi-ligand endocytic receptor that is expressed in many different tissues but primarily in absorptive epithelial tissues such as the kidney. LRP2 mediates uptake of Apo-J which is a binding protein for Amyloid beta. Megalin has a large amino-terminal extracellular domain, a single transmembrane domain, and a short carboxy-terminal cytoplasmic tail. The extracellular ligand-binding-domains bind diverse macromolecules including albumin, apolipoproteins B and E, and lipoprotein lipase. Megalin is critical for the reuptake of numerous ligands, including lipoproteins, sterols, vitamin-binding proteins, and hormones. It also has a role in cell-signaling; extracellular ligands include parathyroid hormones and the morphogen sonic hedgehog while cytosolic ligands include MAP kinase scaffold proteins and JNK interacting proteins. Recycling of this membrane receptor is regulated by phosphorylation of its cytoplasmic domain. Mutations in the LRP2 gene cause Donnai-Barrow syndrome (DBS) and facio-oculoacoustico-renal syndrome (FOAR).
Immunogen
This monoclonal antibody was raised against purified human LRP2 protein.