Reactivity | HuSpecies Glossary |
Applications | WB, ELISA(Det) |
Clonality | Polyclonal |
Host | Goat |
Conjugate | Biotin |
Concentration | LYOPH |
Immunogen | Mouse myeloma cell line NS0-derived recombinant human LOX-1 (R&D Systems, Catalog # 1798-LX) Ser61-Gln273 Accession # P78380 |
Specificity | Detects human LOX-1 in ELISAs and Western blots. In sandwich immunoassays, less than 0.1% cross-reactivity with recombinant mouse LOX‑1 is observed. |
Source | N/A |
Isotype | IgG |
Clonality | Polyclonal |
Host | Goat |
Gene | OLR1 |
Purity Statement | Antigen Affinity-purified |
Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
Dilutions |
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Application Notes | ELISA Capture: Human LOX-1/OLR1 Antibody (Catalog # MAB17981) ELISA Detection: Human LOX-1/OLR1 Biotinylated Antibody (Catalog # BAF1798) Standard: Recombinant Human LOX-1/OLR1 (Catalog # 1798-LX) |
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Readout System | ||
Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Preservative | No Preservative |
Concentration | LYOPH |
Reconstitution Instructions | Reconstitute at 0.2 mg/mL in sterile PBS. |
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 human LOX-1 gene encodes a 273 amino acid (aa) residue protein with a short N-terminal intracellular domain, a transmembrane domain, an extracellular stalk/neck region followed by a C-type lectin-like domain (CTLD) (1, 6). 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. Human 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.
Secondary Antibodies |
Isotype Controls |
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