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Recombinant Cynomolgus Monkey LDLR His-tag Protein, CF

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When Human LDL is immobilized at 4.00 µg/mL (100 µL/well), Recombinant Cynomolgus Monkey LDLR His-tag Protein (Catalog # 11151-LD) binds with an ED50 of 30.0‑300 ng/mL.
2 μg/lane of Recombinant Cynomolgus Monkey LDLR His-tag Protein (Catalog # 11151-LD) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, ...read more

Product Details

Summary
Reactivity Pm-CmSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Cynomolgus Monkey LDLR His-tag Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Human LDL is immobilized at 4.00 µg/mL (100 µL/well), Recombinant Cynomolgus Monkey LDLR His-tag (Catalog # 111151-LD) binds with an ED50 of 30.0-300 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived cynomolgus monkey LDLR protein
Ala22-Gly788, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Ala22
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
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
125-140 kDa, under 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 with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 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 Cynomolgus Monkey LDLR His-tag 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 (LDLR) is the founding member of the LDLR family, a group of widely expressed type I transmembrane glycoprotein cell surface scavenger receptors (1-5). Members of the family are endocytic receptors which bind and internalize extracellular ligands, including lipoproteins, exotoxins, and lipid‑carrier complexes but can also co-regulate adjacent cell-surface signaling molecules (3, 4). Mature LDLR consists of an extracellular domain (ECD) with 7 cysteine‑rich complement-like repeats (class A LDL domains), calcium-binding EGF repeats, and beta ‑propeller structures (class B LDL repeats), a transmembrane domain and a cytoplasmic domain with an NPxY-repeat motif. The ECD of cynomologus LDLR shares 94% amino acid sequence identity with human LDLR. LDLR is constitutively and widely expressed and plays a key role in regulating cholesterol homeostasis. The class A LDL domains near the N-terminus of LDLR bind apoB and apoE, the apolipoproteins of low- and very low-density lipoproteins (LDL and VLDL), respectively (1, 2, 4, 7). Hepatocyte LDLR is responsible for endocytosis and clearing of most plasma LDL cholesterol from circulation (2, 7). At the low pH of the endocytic vesicle, it dissociates, allowing degradation of LDL and recycling of LDLR to the cell surface (1, 4). Lack of LDLR expression or function causes familial hypercholesterolemia (FH) and leads to premature cardiovascular disease (4, 7, 8). The protease PCSK9 (proprotein convertase subtilisin/kexin type 9) can also cause increased plasma cholesterol by promoting LDLR degradation rather than recycling to the cell surface (8-10). Additionally, soluble forms of LDLR are reported to be released by phorbol esters or interferons and could serve as a disease marker (5, 11, 12). Several studies have demonstrated a role for LDLR in cancer progression, including liver cancer, leukemia, lung cancer, breast cancer, colorectal cancer, and prostate cancer (13).
  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. Begg, M.J. et al. (2004) Eur. J. Biochem. 271:524.
  6. Stolt, P.C. and H.H. Bock (2006) Cell. Signal. 18:1560.
  7. Defesche, J.C. (2004) Semin. Vasc. Med. 4:5.
  8. De Castro-Oros, I. et al. (2010) Appl. Clin Genet. 3:53.
  9. Zhang, D.W. et al. (2008) Proc. Natl. Acad. Sci. U.S.A. 105:13045.
  10. Tavori, H. et al. (2013) Circulation 127:2403.
  11. Fischer, D.G. et al. (1993) Science 262:250.
  12. Mbikay, M. et al. (2020) Lipids Health Dis 19:17
  13. Roslan, Z. et al. (2019) J. Oncol. 2019:536302.

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