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Recombinant Mouse LDLR Protein, CF

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When Human LDL is immobilized at 5 μg/mL (100 μL/well),Recombinant Mouse LDLR (Catalog # 2255-LD/CF) binds with an ED50 of 0.4‑4 μg/mL.

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

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Recombinant Mouse LDLR Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Human LDL is immobilized at 5 μg/mL (100 μL/well), the concentration of Recombinant Mouse LDLR that produces 50% of the optimal binding response is 0.4‑4 μg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse LDLR protein
Ala22-Arg790 (Ala23Val and Cys27Gly), with a C-terminal 10-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
  • Binding Activity
Theoretical MW
85.7 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
130-135 kDa, reducing conditions
Publications
Read Publication using
2255-LD/CF 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 Trehalose.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 200 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Mouse LDLR 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 mouse LDL R ECD shares 78%, 86%, 76% and 76% aa sequence identity with human, 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. Polvino, W.J. et al. (1992) Somat. Cell Mol. Genet. 18:443.
  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 (2255-LD/CF)(1)

We have publications tested in 1 confirmed species: Mouse.

We have publications tested in 1 application: Bioassay.


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Bioinformatics

Gene Symbol Ldlr
Uniprot