ApoA5 antibodies are immunoreagents designed to bind specifically to the ApoA5 protein, a liver-derived apolipoprotein that modulates plasma triglyceride levels by influencing lipoprotein lipase (LPL) activity and very-low-density lipoprotein (VLDL) production . These antibodies are pivotal for:
Protein detection: Identifying ApoA5 in tissues (e.g., liver, small intestine) and plasma fractions .
Mechanistic studies: Elucidating ApoA5’s role in triglyceride homeostasis and its interaction with regulatory complexes like ANGPTL3/8 .
Disease research: Investigating hypertriglyceridemia and metabolic syndrome linked to ApoA5 dysfunction .
ApoA5 antibodies vary in host species, clonality, and applications. Below is a comparison of notable commercial and research-grade ApoA5 antibodies:
Western blot (WB): Detects ApoA5 at ~41 kDa (precursor) and 39 kDa (mature form) .
Immunoprecipitation (IP): Isolates ApoA5 complexes for interaction studies .
Immunofluorescence: Localizes ApoA5 in hepatocytes and lipid droplets .
ApoA5 antibodies confirmed that hepatic ApoA5 deficiency increases plasma triglycerides by reducing LPL activity and promoting lipid droplet accumulation in hepatocytes .
Studies using CT-APOA5 pAb demonstrated that C-terminal sequences of ApoA5 are essential for suppressing ANGPTL3/8-mediated LPL inhibition .
In Apoa5−/− mice, recombinant ApoA5 restored intravascular LPL levels and reduced triglycerides by 86% (from 1,116 to 87 mg/dL) .
An inhibitory ANGPTL3/8 antibody (IBA490) mimicked ApoA5’s function, normalizing triglyceride levels in mice .
Double immunofluorescence with ApoA5 antibodies revealed that olanzapine-induced hypertriglyceridemia correlates with ApoA5 accumulation in lipid droplets rather than plasma membranes .
ApoA5 antibodies are indispensable for: