OLR1 Human, HEK
Description
Functional Insights from HEK-Expressed OLR1
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Signaling Pathways: OLR1 activates NF-κB, ERK1/2, and p38 MAPK pathways, contributing to endothelial dysfunction and atherosclerosis .
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Ligand Interactions: Binds oxidized LDL (ox-LDL), CRP, and fibronectin, facilitating foam cell formation and plaque instability .
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Soluble LOX-1 (sLOX-1): HEK293 cells transfected with OLR1 secrete sLOX-1, a biomarker for acute coronary syndromes .
Key Findings in HEK Models
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Proteolytic Shedding: HEK293 cells release sLOX-1 without thrombin stimulation, suggesting constitutive shedding mechanisms .
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Oligomerization: NTFs (N-terminal fragments) of OLR1 dimerize to activate MAPK pathways independently of ligand binding .
Comparative Advantages of HEK-Produced OLR1
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Native Glycosylation: HEK systems preserve post-translational modifications absent in bacterial expression, enhancing ligand-binding accuracy .
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Stability: Lyophilized HEK-produced OLR1 remains stable at -20°C for long-term storage .
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Relevance to Human Physiology: Retains structural and functional homology to endogenous human OLR1 .
Clinical and Diagnostic Implications
Product Specs
Oxidized low density lipoprotein (lectin-like) receptor 1, CLEC8A, hLOX1, SCARE1, Lectin-type oxidized LDL receptor 1, Lectin-like oxidized LDL receptor 1, C-type lectin domain family 8 member A, LOXIN, SLOX1, ox LDL receptor 1, Oxidized low-density lipoprotein receptor 1 soluble form, scavenger receptor class E member 1, SR-E1.
Product Science Overview
The OLR1 gene is located on chromosome 12 (12p13.2) in humans . The gene is regulated through the cyclic AMP signaling pathway and can produce multiple transcript variants through alternative splicing . The protein itself is a type II membrane protein with a C-type lectin-like domain, which is responsible for binding oxLDL .
LOX-1 is primarily expressed on endothelial cells, macrophages, and smooth muscle cells . Under normal conditions, the expression of LOX-1 on endothelial cells is relatively low. However, it can be significantly upregulated by various atherosclerotic stimuli such as tumor necrosis factor-alpha (TNF-α), oxLDL, and blood vessel shear stress .
The primary function of LOX-1 is to bind, internalize, and degrade oxLDL . OxLDL is a marker of atherosclerosis and induces vascular endothelial cell activation and dysfunction, leading to pro-inflammatory responses, oxidative stress, and apoptosis . LOX-1 also plays a role in the regulation of Fas-induced apoptosis .
Mutations and dysregulation of the OLR1 gene have been associated with several cardiovascular diseases, including atherosclerosis and myocardial infarction . The receptor’s role in endothelial dysfunction and plaque formation makes it a critical target for understanding and potentially treating these conditions .
Additionally, LOX-1 has been implicated in other pathological processes, such as Alzheimer’s disease, due to its involvement in oxidative stress and inflammation .
Human recombinant LOX-1, produced in HEK (Human Embryonic Kidney) cells, is widely used in research to study its structure, function, and role in disease. This recombinant protein allows for detailed biochemical and biophysical analyses, facilitating the development of therapeutic strategies targeting LOX-1 .
