Human Lipoprotein, Very Low Density (VLDL)
Native whole molecule
Produktdetails
Synonyms
VLDL
Description of Human Lipoprotein, Very Low Density (VLDL)
Human Lipoprotein, Very Low Density (VLDL) is a 10-80000000 Da protein. Very low-density lipoprotein (VLDL) is a triglyceride-rich lipoprotein synthesized and secreted by the liver, with typical fasting concentrations ranging from 0.5 to 2.0 g/L. VLDL’s primary function is to transport endogenous triglycerides, cholesterol, and other lipids from the liver to peripheral tissues, where they are either utilized for energy or stored. Structurally, VLDL contains apolipoprotein B-100, which is essential for its assembly, secretion, and recognition by cellular receptors. As VLDL circulates, it interacts with enzymes such as lipoprotein lipase, which hydrolyzes its triglycerides, transforming VLDL into intermediate-density lipoprotein (IDL) and eventually low-density lipoprotein (LDL). Beyond lipid transport, VLDL influences vascular function by modulating nitric oxide signaling and stimulating aldosterone synthesis, affecting blood pressure regulation. Elevated VLDL levels are linked to atherosclerosis, coronary artery disease, metabolic syndrome, and type 2 diabetes, especially when large or electronegative VLDL subclasses are present. Clinically, VLDL measurement aids in cardiovascular risk assessment and research into lipid metabolism and cardiometabolic disorders.
Source
Prepared from fresh, non-frozen plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests.
Storage
For long term, store Human Lipoprotein, Very Low Density (VLDL) at +2 to 8°C.
Applications
Cardiovascular Disease, Diabetes.
Citations/Publications
Liu, C. C., et al., (2022), 'Peripheral apoE4 enhances Alzheimer’s pathology and impairs cognition by compromising cerebrovascular function', Nature Neuroscience. 25: pp 1020–1033. Available at: https://doi.org/10.1038/s41593-022-01127-0
Gunn, K. H., et al., (2023), 'Structure of dimeric lipoprotein lipase reveals a pore adjacent to the active site', Nature Communications 14: pp 2569. Available at: https://doi.org/10.1038/s41467-023-38243-9
Moreno-Gordaliza, E., et al., (2016), 'A novel method for serum lipoprotein profiling using high performance capillary isotachophoresis', Analytica Chimica Acta 944: pp 57-69. Available at: http://dx.doi.org/10.1016/j.aca.2016.09.038
Zhong, C. C., et al., (2018), 'Pharmacokinetics and disposition of anlotinib, an oral tyrosine kinase inhibitor, in experimental animal species', Acta Pharmacologica Sinica 39: pp 1048–1063. Available at: doi: 10.1038/aps.2017.199;
Nimonkar, A. V., et al., (2019), 'A lipoprotein lipase–GPI-anchored high-density lipoprotein–binding protein 1 fusion lowers triglycerides in mice: Implications for managing familial chylomicronemia syndrome', J. Biol. Chem. 295(10): pp 2900–2912. Available at: DOI 10.1074/jbc.RA119.011079
Shipped with ice packs
Gel Scan of Human Lipoprotein, Very Low Density (VLDL)
Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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Payment Methods
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