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Recombinant Human LDLR (High Purity) Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human LDLR (High Purity) Protein, CF Summary

Details of Functionality
Measured in a competitive binding assay. When human LDL is immobilized at 1 μg/mL (100 μL/well), Recombinant Human LDL R inhibits 50% binding of biotinylated recombinant human LDL R (0.5 μg/mL) at the concentration range of 0.3-1.5 μg/mL
Source
Mouse myeloma cell line, NS0-derived human LDL R protein
Ala22-Arg788, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Ala22
Protein/Peptide Type
Recombinant Proteins
Gene
LDLR
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
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
120-145 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.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human LDLR (High Purity) Protein, CF

  • FH
  • FHC
  • LDL R
  • LDL receptor
  • LDLCQ2
  • LDLR
  • low density lipoprotein receptor
  • low-density lipoprotein receptor class A domain-containing protein 3
  • low-density lipoprotein receptor

Background

The low density lipoprotein receptor (LDL R) is the founding member of the LDL R family of widely expressed cell surface scavenger receptors (1-5). Members of the family are endocytic receptors, but can also co-regulate adjacent cell-surface signaling molecules (3, 4). Many proteins in the LDL R family are cleaved by extracellular proteases to release soluble forms to the circulation, and many of these soluble forms are active (1, 6). Mature LDL R is a 120-160 kDa (depending on glycosylation) type I transmembrane glycoprotein that contains cysteine-rich complement-like repeats (class A LDL domains), calcium-binding EGF repeats, and beta ‑propeller structures (class B LDL repeats) in the extracellular domain (ECD) (1-7). A membrane-proximal Ser/Thr-rich region shows extensive O-linked glycosylation (4, 8). A cytoplasmic NPxY motif links the LDL R to clathrin pits for endocytosis, and binds to select adaptor proteins (1, 4, 8). The human LDL R ECD shares 78%, 76%, 81% and 82% aa sequence identity with mouse, rat, bovine, and porcine LDL R, respectively. LDL R is constitutively and widely expressed. Its class A LDL domains near the N-terminus bind apoB and apoE, the apolipoproteins of low- and very low-density lipoproteins (LDL and VLDL), respectively (1, 2, 4, 9). Hepatocyte LDL R is responsible for endocytosis and clearing of most plasma LDL cholesterol (2, 9). At the low pH of the endocytic vesicle, it dissociates, allowing degradation of LDL and recycling of LDL R to the cell surface (1, 4). Lack of LDL R expression or function causes familial hypercholesterolemia (FH) (4, 9, 10). The protease PCSK9 (proprotein convertase subtilisin/kexin type 9) can also cause increased plasma cholesterol by promoting LDL R degradation rather than recycling to the cell surface (10-12). Soluble forms of approximately 140 kDa and 28 kDa are reported to be released by phorbol esters or interferons, respectively (6, 7).
  1. Go, G.W. and A. Mani (2012) Yale J. Biol. Med. 85:19.
  2. Ren, G. et al. (2010) Proc. Natl. Acad. Sci. USA 107:1059.
  3. Bujo, H. and Y. Saito (2006) Arterioscler. Thromb. Vasc. Biol. 26:1246.
  4. Gent, J. and I. Braakman (2004) Cell. Mol. Life Sci. 61:2461.
  5. Yamamoto, T. et al. (1984) Cell 39:27.
  6. Begg, M.J. et al. (2004) Eur. J. Biochem. 271:524.
  7. Fischer, D.G. et al. (1993) Science 262:250.
  8. Stolt, P.C. and H.H. Bock (2006) Cell. Signal. 18:1560.
  9. Defesche, J.C. (2004) Semin. Vasc. Med. 4:5.
  10. De Castro-Oros, I. et al. (2010) Appl. Clin Genet. 3:53.
  11. Zhang, D.W. et al. (2008) Proc. Natl. Acad. Sci. USA 105:13045.
  12. Tavori, H. et al. (2013) Circulation 127:2403.

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Bioinformatics

Gene Symbol LDLR
Uniprot