Purity
>85%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its binding ability in a functional ELISA.
When Recombinant Mouse LRPAP (Catalog # 4480-LR) is coated at 1 μg/mL (100 μL/well), the concentration of Recombinant Mouse VLDL R that produces 50% of the optimal binding response is found to be approximately 0.01‑0.05 μg/mL.
Alternately, when Recombinant Mouse VLDL R is coated at 2.5 μg/mL (100 μL/well), the concentration of Recombinant Mouse Reelin (Catalog # 3820-MR) that produces 50% of the optimal binding response is found to be approximately 0.5-2.5 μg/mL.
Source
Mouse myeloma cell line, NS0-derived Thr25-Ala798, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
AnalysisThr25
Predicted Molecular Mass
86.4 kDa
SDS-PAGE
130-175 kDa, reducing conditions
2258-VL |
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Formulation Lyophilized from a 0.2 μm filtered solution in PBS. | ||
Reconstitution Reconstitute at 100 μg/mL in sterile PBS. | ||
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | ||
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Background: VLDL R
VLDL R is a 130 kDa type I transmembrane protein in the LDL receptor family that plays a significant role in lipid metabolism and in nervous system development and function (1, 2). Mouse VLDL R has a 774 aa extracellular domain (ECD) (aa 25 ‑ 798) and a 54 aa cytoplasmic domain. The ECD contains eight LDLR class A repeats, three EGF‑like domains, six LDLR class B repeats, and a juxtamembrane region that is rich in O‑linked glycosylation (3, 4, 5). The cytoplasmic domain contains one NPXY internalization motif. Mouse VLDL R has at least one 105 kDa alternative splice form. This variant (termed type II VLDL R) shows an Arg substitution for aa 751 ‑ 779, and has been associated with endothelial cells (5, 6). The VLDL R expressed here corresponds to a polymorphic form that shows a Cys at position 297 of the precursor. This generates a disulfide bond in the 7th LDL class A domain that is not present when position 297 is occupied by Ser (SwissProt # P98156). The 7th domain is suggested to be a critical determinant of apoE binding to VLDL R (7). VLDL R is predominantly expressed in striated muscle, adipose tissue, brain, and endothelial cells lining capillaries and small arterioles (3, 4, 8, 9). 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) (8, 10). VLDL R binds and internalizes lipoprotein lipase (LPL) and mediates its transport from the basolateral to the lumenal face of endothelial cells (9, 11). VLDL R knockout mice are characterized by reduced LPL activity, reduced serum triglyceride clearance, and a resistance to developing obesity (10, 12, 13). VLDL R influences breast cancer cell motility by mediating the uptake of uPAR‑PAI1 complexes (9, 14). Lipoprotein accumulation via macrophage VLDL R is instrumental in promoting the formation of atherosclerotic plaques (15). In the nervous system, VLDL R and ApoE R2 interactions with reelin are critical for neuronal migration and positioning in the developing brain (16). VLDL R also functions in adult hippocampal synapse maturation, synaptic plasticity, and memory formation (17, 18). 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.
References:
Qiu, S. et al. (2006) Neurobiol. Learn. Mem. 85:16.
May, P. et al. (2005) Cell. Mol. Life Sci. 62:2325.
Gafvels, M.E. et al. (1994) Endocrinology 135:387.
Oka, K. et al. (1994) Eur. J. Biochem. 224:975.
Martensen, P.M. et al. (1997) Eur. J. Biochem. 248:583.
GenBank Accession # NP_001154892.
Ruiz, J. et al. (2005) J. Lipid Res. 46:1721.
Wyne, K.L. et al. (1996) Arterioscler. Thromb. Vasc. Biol. 16:407.
Argraves, K.M. et al. (1995) J. Biol. Chem. 270:26550.
Goudriaan, J.R. et al. (2001) Arterioscler. Thromb. Vasc. Biol. 21:1488.
Obunike, J.C. et al. (2001) J. Biol. Chem. 276:8934.
Yagyu, H. et al. (2002) J. Biol. Chem. 277:10037.
Goudriaan, J.R. et al. (2004) J. Lipid Res. 45:1475.
Webb, D.J. et al. (1999) J. Biol. Chem. 274:7412.
van Eck, M. et al. (2005) Atherosclerosis 183:230.
Jossin, Y. et al. (2004) J. Neurosci. 24:514.
Niu, S. et al. (2004) Neuron 41:71.
Weeber, E.J. et al. (2002) J. Biol. Chem. 277:39944.
Long Name:
Very Low Density Lipoprotein Receptor
Entrez Gene IDs:
7436 (Human); 22359 (Mouse)
Alternate Names:
CARMQ1; CHRMQ1; FLJ35024; very low density lipoprotein receptor; very low-density lipoprotein receptor; VLDL R; VLDL receptor; VLDLR; VLDL-R; VLDLRCH
