Mouse LOX-1/OLR1 C-Terminus Biotinylated Antibody

Applications

Mouse LOX-1/OLR1 Sandwich Immunoassay

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: LOX-1/OLR1

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 up‑regulates 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 down‑regulation 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.

Product Datasheets

Related Research Areas

• C-type Lectin Family
• C-type Lectin Receptors
• HIF Transcription Factors
• Lipid/Cholesterol Metabolism
• Lipoprotein Receptors and Associated Proteins
• Obesity
• Preeclampsia
• Scavenger Receptors
• Uptake and Transport Molecules in VSMC
• Uptake and Transport Molecules on Endothelial Cells