Recombinant Human VLDLR Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 8444-VL

R&D Systems, part of Bio-Techne
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8444-VL-025
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Key Product Details

Source

HEK293

Accession #

P98155

Conjugate

Unconjugated

Applications

Bioactivity

View all VLDLR Proteins and Enzymes »

Product Specifications

Source

Human embryonic kidney cell, HEK293-derived human VLDL R protein
Thr25-Ser797, with a C-terminal 6-His tag

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Thr25

Predicted Molecular Mass

86 kDa

SDS-PAGE

116-142 kDa, reducing conditions

Activity

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.

Scientific Data Images for Recombinant Human VLDLR Protein, CF

Recombinant Human VLDLR Protein SDS-PAGE

Recombinant Human VLDLR Protein SDS-PAGE

1 μg/lane of Recombinant Human VLDL R (Catalog # 8444-VL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing bands at 129 and 107 kDa, respectively.

Formulation, Preparation and Storage

8444-VL
Formulation Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Reconstitution
Reconstitute at 250 μg/mL in sterile PBS.

Reconstitution Buffer Available:
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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.
  • 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.

Background: VLDLR

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).

References

  1. May, P. et al. (2005) Cell. Mol. Life Sci. 62:2325.
  2. Sakai, J. et al. (1994) J. Biol. Chem. 269:2173.
  3. Iijima, H. et al. (1998) J. Biochem. 124:747.
  4. Ruiz, J. et al. (2005) J. Lipid Res. 46:1721.
  5. Wyne, K.L. et al. (1996) Arterioscler. Thromb. Vasc. Biol. 16:407.
  6. Hauser, P.S. et al. (2011) Prog. Lipid Res. 50:62.
  7. Argraves, K.M. et al. (1995) J. Biol. Chem. 270:26550.
  8. Obunike, J.C. et al. (2001) J. Biol. Chem. 276:8934.
  9. Yagyu, H. et al. (2002) J. Biol. Chem. 277:10037.
  10. Webb, D.J. et al. (1999) J. Biol. Chem. 274:7412.
  11. van Eck, M. et al. (2005) Atherosclerosis 183:230.
  12. Hiesberger, T. et al. (1999) Neuron 24:481.
  13. Trommsdorff, M. et al. (1999) Cell 97:689.
  14. Weeber, E.J. et al. (2002) J. Biol. Chem. 277:39944.

Long Name

Very Low Density Lipoprotein Receptor

Alternate Names

CHRMQ1, VLDL R, VLDLRCH

Entrez Gene IDs

7436 (Human); 22359 (Mouse)

Gene Symbol

VLDLR

UniProt

P98155

Additional VLDLR Products

Product Documents for Recombinant Human VLDLR Protein, CF

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Product Specific Notices for Recombinant Human VLDLR Protein, CF

For research use only

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