Mouse VLDLR Biotinylated Antibody

VLDL R is a 105 kDa type I integral membrane protein that belongs to the LDL receptor family. It plays a significant role in lipid metabolism and in nervous system development and function (1, 2). Mouse VLDL R has a 770 amino acid (aa) extracellular domain (ECD) and a 54 aa cytoplasmic region. The ECD contains eight LDLR class A repeats, three EGF-like repeats, six LDLR class B repeats, and a juxtamembrane region that is rich in O-linked glycosylation (3, 4). The cytoplasmic domain contains one NPXY internalization motif. VLDL R is predominantly expressed in striated muscle, adipose tissue, brain, and endothelial cells lining capillaries and small arterioles (3-6). VLDL R participates in the tissue uptake of fatty acids from plasma by mediating the internalization of ApoE-containing lipoparticles (i.e. VLDL, beta‑VLDL, and chylomicron remnants) (5, 7). VLDL R binds and internalizes lipoprotein lipase (LPL) and mediates its transport from the basolateral to the lumenal face of endothelial cells (6, 8). VLDL R knockout mice are characterized by reduced LPL activity, reduced serum triglyceride clearance, and a resistance to developing obesity (7, 9, 10). VLDL R influences breast cancer cell motility by mediating the uptake of uPAR-PAI1 complexes (6, 11). Lipoprotein accumulation via macrophage VLDL R is instrumental in promoting the formation of atherosclerotic plaques (12). In the nervous system, VLDL R and ApoE R2 interactions with Reelin are critical for neuronal migration and positioning in the developing brain (13). VLDL R also functions in adult hippocampal synapse maturation, synaptic plasticity, and memory formation (14, 15). The ECD of mouse VLDL R shares 95% aa sequence identity with human and rat VLDL R. Within shared regions, mouse VLDL R shares 55% and 53% aa sequence identity with ApoE R2 and LDL R, respectively.