Refolding and characterization of the functional ligand-binding domain of human lectin-like oxidized LDL receptor

Anti-LOX-1 therapy in rats with diabetes and dyslipidemia: ablation of renal vascular and epithelial manifestations

“…This effect was probed with an anti-LOX-1 blocking polyclonal antibody, which was designed to impede oxLDL binding to LOX-1 by blocking the extracellular binding domain of rat LOX-1. This particular peptide site was targeted because it is a component of the unique lectin-binding domain required for LOX-1 binding activity (8,48). The binding portion of LOX-1 is homologous to the antigen recognition site of NK cells (9), and it may have originated from duplication of an ancestral gene (49).…”

Accurate quantitation for in vitro refolding of single domain antibody fragments expressed as inclusion bodies by referring the concomitant expression of a soluble form in the periplasms of Escherichia coli

“…In papers dealing with refolding proteins other than antibodies or their fragments, there are several methods, a 'functional assay', in addition to the absorbance (A 280 ) as usual, as described above [19], such as the enzymatic activity of an authentic sample [20], recovery yield of the cell lysate [21], or the receptor-ligand binding assay [22].…”

Decreased Lectin-Like Oxidized LDL Receptor 1 (LOX-1) and Low Nrf2 Activation in Placenta Are Involved in Preeclampsia

“…LOX-1 is synthesized as a precursor form and processed into mature form by glycosylation (28). Xie et al (29) found that the extracellular C-terminal lectin-like domain is sufficient for the binding to oxLDL, and this domain is not glycosylated, which suggests the glycosylation of LOX-1 is not a prerequisite for the binding of ligand. Accordingly, we regarded these three signals as functional LOX-1 and quantified.…”