Apolipoprotein AII
16-16-120102
Protein IDP02652
Product group Proteins / Signaling Molecules
Overview
- SupplierAthens Bioscience
- Product NameApolipoprotein AII
- Delivery Days Customer9
- Applications SupplierIn Vitro Diagnostic, Cardiovascular Research
- CertificationResearch Use Only
- Estimated Purity≥95% by SDS-PAGE. Single band on polyacrylamide electrophoresis under reduced conditions.
- Protein IDP02652
- Protein NameApolipoprotein A-II
- Scientific DescriptionApolipoprotein A-II (ApoA-II), constituting 25% of HDL-associated apolipoproteins, circulates in plasma at 30–50 mg/100 mL. This 17.4 kDa protein stabilizes HDL structure and modulates lipid metabolism, though its physiological role remains debated. ApoA-II inhibits lecithin-cholesterol acyltransferase (LCAT) and cholesteryl ester transfer protein (CETP), influencing HDL remodeling and cholesterol efflux. While some studies suggest proatherogenic effects via reduced HDL antioxidant capacity, large prospective cohorts demonstrate an inverse correlation between ApoA-II levels and coronary artery disease (CAD) risk, independent of HDL cholesterol. Alcohol consumption increases ApoA-II production, correlating with elevated HDL-C and potential cardioprotection. Genetic variants like APOA2 rs5082 interact with saturated fat intake, modulating obesity and type 2 diabetes risk. Clinically, ApoA-II deficiency shows minimal lipid disruption, whereas elevated levels associate with hypertriglyceridemia, insulin resistance, and pancreatic cancer biomarker potential. Emerging therapies target ApoA-II’s role in amyloidosis inhibition and HDL particle engineering for atherosclerosis management. Despite conflicting mechanistic insights, ApoA-II remains a critical player in HDL dynamics and metabolic disease pathways.
- Shelf life instructionmore then 1 year
- SourceSource human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
- Storage Instruction-80C
- UNSPSC41116100
References
- Deng, M. et al., (2018), 'LILRB4 signalling in leukaemia cells mediates T cell suppression and tumour infiltration', Nature, 562: pp 605–609.Read this paper
- Yamauchi, K., et al., (2020), 'The redox status of cysteine thiol residues of apolipoprotein E impacts on its lipid interactions', Biol. Chem., 401(5): pp 617–627.Read this paper
- Negi, P., et al., (2016), 'Identification and analysis of anti-HDL scFv-antibodies obtained from phage display based synthetic antibody library', Clinical Biochemistry 49: pp 472–479.Read this paper
- Matsuura, H., et al., (2024), 'Apolipoprotein E isoforms and their Cys-thiol modifications impact LRP1-mediated metabolism of triglyceride-rich lipoproteins.', FEBS Lett, 598: pp 347-362.Read this paper