Reactivity | HuSpecies Glossary |
Applications | Flow |
Clone | 331212 |
Clonality | Monoclonal |
Host | Mouse |
Conjugate | PerCP (Peridinin-chlorophyll Protein Complex) |
Immunogen | Mouse myeloma cell line NS0-derived recombinant human LOX-1/OLR1 Ser61-Gln273 Accession # P78380 |
Specificity | Detects human LOX-1 in direct ELISAs and Western blots. In direct ELISAs and Western blots, this antibody does not cross-react with recombinant mouse LOX‑1. |
Source | N/A |
Isotype | IgG2b |
Clonality | Monoclonal |
Host | Mouse |
Gene | OLR1 |
Purity Statement | Protein A or G purified from hybridoma culture supernatant |
Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
Storage | Store the unopened product at 2 - 8° C. Do not use past expiration date. Protect from light. |
Buffer | Supplied in a saline solution containing BSA and Sodium Azide. |
Preservative | Sodium Azide |
Lectin-like oxidized low-density-lipoprotein receptor-1 (LOX-1), also known as oxidized low-density-lipoprotein receptor-1 (OLR-1), is a 40-50 kDa 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 a founding 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, and 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 a covalent homodimer, that can further associate into a non-covalent-linked oligomer (9). Cell surface LOX-1 can also be cleaved by MMPs (such as MMP-1, -2, or -14) to release a soluble 32-34 kDa LOX-1 extracellular domain (10). 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 (11). 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. Over amino acids (aa) 61-273, human LOX-1 shares 61% aa sequence identity with mouse LOX-1 (adjusted for a large insert found in the mouse ECD).
Secondary Antibodies |
Isotype Controls |
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