Recombinant Human LDLR Protein

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity

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Recombinant Human LDLR Protein Summary

Additional Information
A New and Improved rh LDL R is Now Available! The new protein has ~50% better activity!
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 0.4-2 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 & Asp193
Protein/Peptide Type
Recombinant Proteins
Gene
LDLR
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.1 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
85.6 kDa & 66.8 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 & 95-110 kDa, reducing conditions
Publications
Read Publications using
2148-LD in the following applications:

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 BSA as a carrier protein.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.

Notes

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

Alternate Names for Recombinant Human LDLR Protein

  • 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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Publications for LDLR (2148-LD)(9)

We have publications tested in 2 confirmed species: Human, Hamster.

We have publications tested in 4 applications: Binding Assay, Bioassay, Enzyme Assay, Surface Plasmon Resonance.


Filter By Application
Binding Assay
(1)
Bioassay
(5)
Enzyme Assay
(1)
Surface Plasmon Resonance
(2)
All Applications
Filter By Species
Human
(8)
Hamster
(1)
All Species
Showing Publications 1 - 9 of 9.
Publications using 2148-LD Applications Species
Y Masuda, S Yamaguchi, C Suzuki, T Aburatani, Y Nagano, R Miyauchi, E Suzuki, N Yamamura, K Nagatomo, H Ishihara, K Okuno, F Nara, G Matschiner, R Hashimoto, T Takahashi, T Nishizawa Generation and Characterization of a Novel Small Biologic Alternative to Proprotein Convertase Subtilisin/Kexin Type 9 (PCSK9) Antibodies, DS-9001a, Albumin Binding Domain-Fused Anticalin Protein J. Pharmacol. Exp. Ther., 2018;365(2):368-378. 2018 [PMID: 29463608] (Bioassay, Human) Bioassay Human
SA Felt, GN Droby, VZ Grdzelishv Ruxolitinib and polycation combination treatment overcomes multiple mechanisms of resistance of pancreatic cancer cells to oncolytic vesicular stomatitis virus J. Virol., 2017;0(0):. 2017 [PMID: 28566376] (Bioassay, Human) Bioassay Human
Kraehling J, Chidlow J, Rajagopal C, Sugiyama M, Fowler J, Lee M, Zhang X, Ramirez C, Park E, Tao B, Chen K, Kuruvilla L, Larrivee B, Folta-Stogniew E, Ola R, Rotllan N, Zhou W, Nagle M, Herz J, Williams K, Eichmann A, Lee W, Fernandez-Hernando C, Sessa W Genome-wide RNAi screen reveals ALK1 mediates LDL uptake and transcytosis in endothelial cells. Nat Commun, 2016;7(0):13516. 2016 [PMID: 27869117] (Enzyme Assay, Human) Enzyme Assay Human
Amirache F, Levy C, Costa C, Mangeot P, Torbett B, Wang C, Negre D, Cosset F, Verhoeyen E Mystery solved: VSV-G-LVs do not allow efficient gene transfer into unstimulated T cells, B cells, and HSCs because they lack the LDL receptor. Blood, 2014;123(9):1422-4. 2014 [PMID: 24578496] (Bioassay, Human) Bioassay Human
Kurasawa J, Shestopal S, Karnaukhova E, Struble E, Lee T, Sarafanov A Mapping the binding region on the low density lipoprotein receptor for blood coagulation factor VIII. J Biol Chem, 2013;288(30):22033-41. 2013 [PMID: 23754288] (Binding Assay, Human) Binding Assay Human
DeVay, Rachel M, Shelton, David L, Liang, Hong Characterization of proprotein convertase subtilisin/kexin type 9 (PCSK9) trafficking reveals a novel lysosomal targeting mechanism via amyloid precursor-like protein 2 (APLP2). J Biol Chem, 2013;288(15):10805-18. 2013 [PMID: 23430252] (Bioassay, Human) Bioassay Human
Duff CJ, Scott MJ, Kirby IT, Hutchinson SE, Martin SL, Hooper NM Antibody-mediated disruption of the interaction between PCSK9 and the low-density lipoprotein receptor. Biochem. J., 2009;419(3):577-84. 2009 [PMID: 19196236] (Surface Plasmon Resonance, Human) Surface Plasmon Resonance Human
Chien YJ, Chen WJ, Hsu WL, Chiou SS Bovine lactoferrin inhibits Japanese encephalitis virus by binding to heparan sulfate and receptor for low density lipoprotein. Virology, 2008;379(1):143-51. 2008 [PMID: 18640695] (Bioassay, Hamster) Bioassay Hamster
Fisher TS, Lo Surdo P, Pandit S, Mattu M, Santoro JC, Wisniewski D, Cummings RT, Calzetta A, Cubbon RM, Fischer PA, Tarachandani A, De Francesco R, Wright SD, Sparrow CP, Carfi A, Sitlani A Effects of pH and low density lipoprotein (LDL) on PCSK9-dependent LDL receptor regulation. J. Biol. Chem., 2007;282(28):20502-12. 2007 [PMID: 17493938] (Surface Plasmon Resonance, Human) Surface Plasmon Resonance Human

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Bioinformatics

Gene Symbol LDLR
Uniprot