Recombinant Mouse VLDLR (Ser297) Protein, CF

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Recombinant Mouse VLDLR (Ser297) Protein, CF Summary

Product Specifications

>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.
Measured by its binding ability in a functional ELISA. Recombinant Mouse VLDLR (Ser297) (Catalog # 2258-VL) binds to Recombinant Mouse LRPAP (Catalog # 4480-LR) with an ED50 of 0.0100‑0.0500 μg/mL.
Mouse myeloma cell line, NS0-derived mouse VLDLR protein
Thr25-Ala798, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Predicted Molecular Mass
86.4 kDa
130-175 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.
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.
  • 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.
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Background: VLDLR

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.

  1. Qiu, S. et al. (2006) Neurobiol. Learn. Mem. 85:16.
  2. May, P. et al. (2005) Cell. Mol. Life Sci. 62:2325.
  3. Gafvels, M.E. et al. (1994) Endocrinology 135:387.
  4. Oka, K. et al. (1994) Eur. J. Biochem. 224:975.
  5. Martensen, P.M. et al. (1997) Eur. J. Biochem. 248:583.
  6. GenBank Accession # NP_001154892.
  7. Ruiz, J. et al. (2005) J. Lipid Res. 46:1721.
  8. Wyne, K.L. et al. (1996) Arterioscler. Thromb. Vasc. Biol. 16:407.
  9. Argraves, K.M. et al. (1995) J. Biol. Chem. 270:26550.
  10. Goudriaan, J.R. et al. (2001) Arterioscler. Thromb. Vasc. Biol. 21:1488.
  11. Obunike, J.C. et al. (2001) J. Biol. Chem. 276:8934.
  12. Yagyu, H. et al. (2002) J. Biol. Chem. 277:10037.
  13. Goudriaan, J.R. et al. (2004) J. Lipid Res. 45:1475.
  14. Webb, D.J. et al. (1999) J. Biol. Chem. 274:7412.
  15. van Eck, M. et al. (2005) Atherosclerosis 183:230.
  16. Jossin, Y. et al. (2004) J. Neurosci. 24:514.
  17. Niu, S. et al. (2004) Neuron 41:71.
  18. 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

Citation for Recombinant Mouse VLDLR (Ser297) Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citation: Showing 1 - 1

  1. PCSK9 is not involved in the degradation of LDL receptors and BACE1 in the adult mouse brain.
    Authors: Liu M, Wu G, Baysarowich J
    J. Lipid Res., 2010-05-07;51(9):2611-8.
    Applications: Western Blot


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