抗LOX-1抗体(Anti-LOX-1, Rat-Mono, PE antibody)

• 価格
• Product Details
• Applications and Data
• Related Product & Information
• Citations

価格

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Product Details

Species Reactivity	Mouse
Label	Phycoerythrin
Immunogen	Mouse myeloma cell line NS0-derived recombinant mouse LOX-1Arg60-Ile363Accession # AAG44998
Source	Monoclonal Rat IgG2A Clone # 214012
Purification	Protein A or G purified from hybridoma culture supernatant
Specificity	Detects mouse LOX-1 in direct ELISAs and Western blots. In these formats, this antibody does not cross-react with recombinant human LOX‑1.

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Applications and Data

	Recommended Concentration	Sample
Flow Cytometry	10 µL/106 cells	See below

Flow Cytometry
	Detection of LOX‑1/OLR1 in RAW 264.7 Mouse Cell Line by Flow Cytometry. 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 histogram). View our protocol for Staining Membrane-associated Proteins.

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Related Product & Information

Background

LOX-1/OLR1

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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 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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Citations

1. Effects of scavenger receptors-1 class A stimulation on macrophage morphology and highly modified advanced glycation end product-protein phagocytosis
   Authors: S Hamasaki, T Kobori, Y Yamazaki, A Kitaura, A Niwa, T Nishinaka, M Nishibori, S Mori, S Nakao, H Takahashi
   Sci Rep, 2018;8(1):5901.
   Species: Mouse
   Sample Type: Whole Cells
   Application: Flow


2. Deletion of LOX-1 Protects against Heart Failure Induced by Doxorubicin
   PLoS ONE, 2016;11(5):e0154994.
   Species: Mouse
   Sample Type: Plasma
   Application: Flow


3. Oxidation by neutrophils-derived HOCl increases immunogenicity of proteins by converting them into ligands of several endocytic receptors involved in antigen uptake by dendritic cells and macrophages.
   Authors: Biedron R, Konopinski M, Marcinkiewicz J, Jozefowski S
   PLoS ONE, 2015;10(4):e0123293.
   Species: Mouse
   Sample Type: Whole Cells
   Application: Flow

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