Recombinant Human LOX 1 protein
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Recombinant Human LOX 1 protein is a Human Fragment protein, in the 61 to 273 aa range, expressed in HEK 293 cells, with >95%, < 0.1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.
View Alternative Names
CLEC8A, LOX1, OLR1, Oxidized low-density lipoprotein receptor 1, Ox-LDL receptor 1, C-type lectin domain family 8 member A, Lectin-like oxidized LDL receptor 1, Lectin-type oxidized LDL receptor 1, LOX-1, Lectin-like oxLDL receptor 1, hLOX-1
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Specifications
Form
Lyophilized
Additional notes
ab152043 was determined to be >95% pure by SEC-HPLC and reducing SDS-PAGE.
General info
Function
Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro-oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram-positive bacteria.. (Microbial infection) May serve as a receptor for adhesin A variant 3 (nadA) of N.meningitidis.
Post-translational modifications
The intrachain disulfide-bonds prevent N-glycosylation at some sites.. N-glycosylated.
Target data
Product promise
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