Recombinant Human VLDLR Protein, CF

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Recombinant Human VLDLR Protein SDS-PAGE
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Product Details
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Recombinant Human VLDLR Protein, CF Summary

Product Specifications

>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.
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 human VLDL R protein
Thr25-Ser797, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Predicted Molecular Mass
86 kDa
116-142 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Reconstitution Reconstitute at 250 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.
  • 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.

Scientific Data

SDS-PAGE Recombinant Human VLDLR Protein SDS-PAGE View Larger

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.

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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).

  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
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


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