>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When Recombinant Human LRPAP is coated at 1 μg/mL (100 μL/well), the concentration of Recombinant Human VLDL R hat produces 50% of the optimal binding response is found to be approximately 5-30 ng/mL.
Human embryonic kidney cell, HEK293-derived Thr25-Ser797, with a C-terminal 6-His tag
1 μg/lane ofRecombinant Human VLDL R (Catalog # 8444-VL)was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditionsand visualized by silver staining, showing bands at 129 and 107kDa, respectively.
Background: VLDL R
Very low density lipoprotein receptor (VLDL R) is a 130 kDa type I transmembrane protein that plays a significant role in lipid metabolism and in nervous system development and function (1). Mature human VLDL R consists of a 770 amino acid (aa) extracellular domain (ECD) with eight tandem LDLR class A repeats, three EGF-like domains, six tandem LDLR class B repeats, and a juxtamembrane region that is rich in O-linked glycosylation; a transmembrane segment, and a 54 aa cytoplasmic domain with one NPxY internalization motif (2). Within the ECD, human VLDLR shares 95% and 92% aa sequence identity with mouse and rat VLDL R, respectively. Alternative splicing of human VLDL R shows a deletion of the O-glycosylated region and also includes a critical determinant for ApoE binding (3, 4). VLDL R is predominantly expressed on endothelial cells lining capillaries and small arterioles (5). 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) (6). VLDL R binds and internalizes lipoprotein lipase (LPL) and mediates its transport from the basolateral to the lumenal face of endothelial cells (7, 8). VLDL R knockout mice are characterized by reduced LPL activity and increased serum triglyceride clearance (9). VLDL R influences breast cancer cell motility by mediating the uptake of uPAR-PAI1 complexes (7, 10). Lipoprotein accumulation via macrophage VLDL R is instrumental in promoting the formation of atherosclerotic plaques (11). In the nervous system, VLDL R and ApoE R2 interactions with Reelin are critical for neuronal migration and positioning in the developing brain (12, 13). VLDL R also functions in adult hippocampal synapse maturation, synaptic plasticity, and memory formation (14).
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Very Low Density Lipoprotein Receptor
Entrez Gene IDs:
7436 (Human); 22359 (Mouse)
CARMQ1; CHRMQ1; FLJ35024; very low density lipoprotein receptor; very low-density lipoprotein receptor; VLDL receptor; VLDLR; VLDL-R; VLDLRCH
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