RAW 264.7 mouse monocyte/macrophage cell line was stained with Rat Anti-Mouse LOX-1/OLR1 PE-conjugated Monoclonal Antibody (Catalog # FAB1564P, filled histogram) or isotype control antibody (Catalog # IC006P, open ...read more
12 months from date of receipt, 2 to 8 °C as supplied.
Buffer
Supplied in a saline solution containing BSA and Sodium Azide.
Preservative
Sodium Azide
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for LOX-1/OLR1 Antibody (214012) [Phycoerythrin]
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 pro‑inflammatory or pro‑atherogenic 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.
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Platt, N. and S. Gordon (1998) Chem. Biol. 5:R193.
Jono, T. et al. (2002) FEBS Lett. 511:170.
Kume, N. et al. (2001) Curr. Opin. Lipidol. 12:419.
Delneste, Y. et al. (2002) Immunity 17:353.
Bruneau, N. et al. (2003) Mol. Biol. Cell 14:2861.
Xie, Q. et al. (2004) DNA and Cell Biol. 23:111.
Chen, J. et al. (2003) Circ. Res. 94:370.
Hoshikawa, H. et al. (1998) Biochem. Biophys. Res. Comm. 245:841.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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