Recombinant Mouse LOX-1/OLR1 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Mouse LOX-1/OLR1 Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized rmLOX-1 at 5 µg/mL (100 µL/well) can bind biotinylated advanced glycation end products of bovine serum albumin (AGE-BSA) with a linear range of 0.02-1 µg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse LOX-1/OLR1 protein
Arg60-Ile363, with an N-terminal 10-His tag
Accession #
N-terminal Sequence
His
Structure / Form
Monomer
Protein/Peptide Type
Recombinant Proteins
Gene
Olr1
Purity
>95%, 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

Theoretical MW
36.3 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
50-60 kDa, reducing conditions
Publications
Read Publications using
1564-LX 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.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 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 LOX-1/OLR1 Protein, CF

  • CLEC8A
  • CLEC8ASLOX1
  • C-type lectin domain family 8 member A
  • hLOX-1
  • Lectin-like oxidized LDL receptor 1
  • Lectin-like oxLDL receptor 1
  • Lectin-type oxidized LDL receptor 1
  • LOX1
  • LOX-1
  • LOX1ox LDL receptor 1
  • LOXIN
  • OLR1
  • oxidised low density lipoprotein (lectin-like) receptor 1
  • oxidized low density lipoprotein (lectin-like) receptor 1
  • oxidized low-density lipoprotein receptor 1
  • oxidized low-density lipoprotein receptor 1, soluble form
  • Ox-LDL receptor 1
  • SCARE1
  • scavenger receptor class E, member 1
  • SR-E1

Background

Lectin-like oxidized low-density-lipoprotein receptor-1 (LOX-1), also known as oxidized low-density-lipoprotein receptor-1 (OLR-1), is a type II transmembrane receptor belonging to the C-type lectin family (1). It also belongs to the functionally defined scavenger receptor (SR) superfamily, whose members share the common ability to bind and internalize modified forms of Low Density Lipoproteins (LDL) (2 - 4). LOX-1 is the first member of the class E scavenger receptor subfamily (SR-E). It binds and supports the internalization of multiple structurally unrelated macromolecules including oxidized LDL, advanced glycation end products (AGE), activated platelets, bacteria, apoptotic or aged cells, and heat shock proteins (5 - 7). LOX-1 has also been implicated as an intestinal receptor involved in the transcytosis of pancreatic bile salt-dependent lipase (8). The mouse LOX-1 gene encodes a 363 amino acid (aa) residue protein with a short N-terminal intracellular domain, a transmembrane domain, triple repeats of an extracellular stalk/neck region followed by a C-type lectin-like domain (CTLD) (11). The CTLD, which is required for ligand recognition, contains the six conserved cysteine residues present in all C-type lectins, but lacks the Ca2+-binding residues found in classical C-type lectins. LOX-1 can be detected on activated endothelial cells, vascular smooth muscle cells, macrophages, intestinal cells and dendritic cells (6 - 8). The expression of LOX-1 is induced by proinflammatory or proatherogenic stimuli, as well as by oxidized LDL itself and hemodynamic or oxidative stress. LOX-1 exists on the cell surface as covalent homodimers, which can further associate into non-covalent-linked oligomers (9). Cell surface LOX-1 can also be cleaved by yet unidentified proteases to release the soluble LOX-1 extracellular domain (6). Binding and endocytosis of oxidized LDL by LOX-1 induces oxidative stress, activates NF kappa B, and upregulates the expression of monocyte chemoattractant protein-1 and matrix metalloproteases (5 - 9). LOX-1-dependent oxidized LDL uptake also induces apoptosis by inducing the expression of the pro-apoptotic Bax and downregulation of the anti-apoptotic Bcl-2 (10). Oxidized LDL plays a key role in the pathogenesis of atherosclerosis and endothelial dysfunction. Blockade of LOX-1 functions may turn out to be a suitable target for the therapeutic intervention of atherosclerosis.

  1. Sawamura, T. et al. (1997) Nature 386:73.
  2. Daugherty, A. (2000) Curr. Opin. Cardiovasc. Pulm. Ren. Invest. Drugs. 2:223.
  3. Platt, N. and S. Gordon (2001) J. Clin. Invest. 108:649.
  4. Platt, N. and S. Gordon (1998) Chem. Biol. 5:R193.
  5. Jono, T. et al. (2002) FEBS Lett. 511:170.
  6. Kume, N. et al. (2001) Curr. Opin. Lipidol. 12:419.
  7. Delneste, Y. et al. (2002) Immunity 17:353.
  8. Bruneau, N. et al. (2003) Mol. Biol. Cell 14:2861.
  9. Xie, Q. et al. (2004) DNA and Cell Biol. 23:111.
  10. Chen, J. et al. (2003) Circ. Res. 94:370.
  11. Hoshikawa, H. et al. (1998) Biochem. Biophys. Res. Comm. 245:841.

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Publications for LOX-1/OLR1 (1564-LX)(2)

We have publications tested in 2 confirmed species: Mouse, N/A.

We have publications tested in 2 applications: Binding Assay, Western Blot.


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Western Blot
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Bioinformatics

Gene Symbol Olr1
Uniprot