Recombinant Human VLDLR Protein, CF Summary
Details of Functionality |
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. |
Source |
Human embryonic kidney cell, HEK293-derived human VLDL R protein Thr25-Ser797, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Thr25 |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
VLDLR |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
86 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
116-142 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 250 μg/mL in sterile PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human VLDLR Protein, CF
Background
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).
- May, P. et al. (2005) Cell. Mol. Life Sci. 62:2325.
- Sakai, J. et al. (1994) J. Biol. Chem. 269:2173.
- Iijima, H. et al. (1998) J. Biochem. 124:747.
- Ruiz, J. et al. (2005) J. Lipid Res. 46:1721.
- Wyne, K.L. et al. (1996) Arterioscler. Thromb. Vasc. Biol. 16:407.
- Hauser, P.S. et al. (2011) Prog. Lipid Res. 50:62.
- Argraves, K.M. et al. (1995) J. Biol. Chem. 270:26550.
- Obunike, J.C. et al. (2001) J. Biol. Chem. 276:8934.
- Yagyu, H. et al. (2002) J. Biol. Chem. 277:10037.
- Webb, D.J. et al. (1999) J. Biol. Chem. 274:7412.
- van Eck, M. et al. (2005) Atherosclerosis 183:230.
- Hiesberger, T. et al. (1999) Neuron 24:481.
- Trommsdorff, M. et al. (1999) Cell 97:689.
- Weeber, E.J. et al. (2002) J. Biol. Chem. 277:39944.
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