Apolipoprotein Detection
Apolipoprotein Detection - Related Videos
10:59
Production of Apolipoprotein C-III Knockout Rabbits using Zinc Finger Nucleases
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Cited by 32 •
2013
Recent development in gene targeting tools makes production of knockout (KO) rabbits possible. In the present work, we generated five Apolipoprotein (Apo) C-III KO rabbits using Zinc Finger Nucleases (ZFN). This work demonstrated that ZFN is a highly efficient method to produce KO rabbits.
07:08
A High Throughput, Multiplexed and Targeted Proteomic CSF Assay to Quantify Neurodegenerative Biomarkers and Apolipoprotein E Isoforms Status
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Cited by 3 •
2016
We describe a high-throughput, multiplex, and targeted proteomic cerebrospinal fluid (CSF) assay developed with potential for clinical translation. The test can quantitate potential markers and risk factors for neurodegeneration, such as the apolipoprotein E variants (E2, E3 and E4), and measure their allelic expression.
07:36
Induction of Atherosclerotic Plaques Through Activation of Mineralocorticoid Receptors in Apolipoprotein E-deficient Mice
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Cited by 8 •
2018
We describe a protocol to induce atherosclerosis in the aortic root of ApoE-/- mice fed with an atherogenic diet, through a continuous release of aldosterone. Methods to characterize plaque composition are also described.
07:37
Click-Chemistry Based Fluorometric Assay for Apolipoprotein N-acyltransferase from Enzyme Characterization to High-Throughput Screening
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Cited by 2 •
2020
Presented here is a sensitive fluorescence assay to monitor apolipoprotein N-acyltransferase activity using diacylglyceryl peptide and alkyne-phospholipids as substrates with click-chemistry.
09:10
Combination of Adhesive-tape-based Sampling and Fluorescence in situ Hybridization for Rapid Detection of Salmonella on Fresh Produce
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Cited by 17 •
2010
This protocol describes a simple adhesive-tape-based approach for sampling of tomato and other fresh produce surfaces, followed by rapid whole cell detection of Salmonella using fluorescence in situ hybridization (FISH).
FAQs
The assay depends on selective binding between an antibody and its target apolipoprotein. When that interaction occurs, the system produces a measurable signal whose intensity is proportional to the target concentration. This relationship allows researchers or clinical laboratories to estimate the amount of a selected protein rather than merely confirm that a lipid-associated protein is present.
Apolipoprotein A-I and apolipoprotein B represent different target proteins within the group of lipid-associated proteins. Measuring them separately provides distinct information about lipoprotein composition and lipid metabolism. Their individual concentrations can therefore support investigations of lipoprotein disorders and cardiovascular risk, while also allowing researchers to examine how different protein components respond to therapeutic interventions.
Immunoassays use antibody recognition to measure a selected apolipoprotein concentration. Electrophoresis separates protein forms, helping reveal differences in their migration or distribution, whereas mass spectrometry identifies protein species through analytical measurement of their molecular characteristics. These methods answer different questions, so combining them can provide complementary information about abundance, separation, and molecular identity.
A sample may contain distinct forms of a lipid-associated protein, and a single concentration measurement may not describe how those forms are distributed. Electrophoresis can resolve these forms, while mass spectrometry can identify them. This added resolution is useful when the research question concerns protein composition or molecular identity rather than only the total amount of a target.
A typical workflow begins by selecting the apolipoprotein or protein form relevant to the question, followed by choosing an approach suited to the desired measurement. An immunoassay can then generate a concentration-related signal, while electrophoresis or mass spectrometry can provide separation or identification. The resulting data are interpreted in relation to lipoprotein structure or lipid metabolism.
This analysis is useful when investigators need to evaluate lipoprotein disorders, examine metabolic pathways, or assess responses to therapeutic interventions. In clinical testing, measurements can contribute to evaluation of lipid-associated cardiovascular risk. In research, comparing selected apolipoproteins or their distinct forms helps connect protein-level findings with changes in lipoprotein structure and metabolism.