For immunochemical detection of ApoB
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ApoB Polyclonal Antibody

Item No. 44650

Technical Information
Synonyms
  • Apolipoprotein B
Immunogen
Purified human ApoB protein
This vial contains 500 µl of goat polyclonal antibody at 2 mg/ml
Storage Buffer
PBS, pH 7.2, with 50% glycerol and 0.02% sodium azide
Host
Goat
Applications
ELISA, IP, WB
Cross Reactivity
(+) ApoB(+) ApoB-48(+) ApoB-100
Species Reactivity
(+) Human(-) Mouse
UniProt Accession №
P04114
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    Product Description

    ApoB is an amphiphilic lipid carrier protein required as the structural component for atherogenic lipoproteins.1 It is expressed as two major forms: a truncated isoform, ApoB-48, which is expressed in the intestines, and full-length ApoB-100, which is expressed in the liver and to a lesser extent by cardiomyocytes.1,2,3 ApoB-100 is composed of βα1, β1, α2, β2, and α3 domains where the β domains are involved in forming irreversible bonds to the lipid core and the α domains have reversible lipid affinity.2 ApoB-48 is incorporated into chylomicrons and their remnants whereas ApoB-100 is incorporated into lipoproteins VLDLs, IDLs, and LDLs.1 Uptake of ApoB-containing lipoproteins is primarily mediated via the LDL receptor (LDLR), heparin sulfate proteoglycans, and scavenger receptor BI (SR-BI). Transgenic mice expressing human APOB and APOA fed an atherogenic diet exhibit increased levels of VLDL- and LDL-cholesterol and increased aortic lesion areas compared with non-transgenic mice.4 Mutations in APOB are associated with autosomal dominant hypercholesterolemia and familial hypobetalipoproteinemia.5,6 Cayman’s ApoB Polyclonal Antibody can be used for immunoprecipitation (IP) and Western blot (WB) applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Behbodikhah, J., Ahmed, S., Elyasi, A., et alApolipoprotein B and cardiovascular disease: Biomarker and potential therapeutic target. Metabolites 11(10), 690 (2021).

    2. Segrest, J.P., Jones, M.K., De Loof, H., et alStructure of apolipoprotein B-100 in low density lipoproteins. J. Lipid. Res. 42(9), 1346-1367 (2001).

    3. Véniant, M.M., Kim, E., McCormick, S., et alInsights into apolipoprotein B biology from transgenic and gene-targeted mice. J. Nutr. 129, 451S-455S (1999).

    4. Callow, M.J., Verstuyft, J., Tangirala, R., et alAtherogenesis in transgenic mice with human apolipoprotein B and lipoprotein (a). J. Clin. Invest. 96(3), 1639-1649 (1995).

    5. van der Graaf, A., Avis, H.J., Kusters, D.M., et alMolecular basis of autosomal dominant hypercholesterolemia: Assessment in a large cohort of hypercholesterolemic children. Circulation 123(11), 1167-1173 (2011).

    6. Gangloff, A., Bergeron, J., Couture, P., et alA novel mutation of apolipoprotein B in a French Canadian family with homozygous hypobetalipoproteinemia. J. Clin. Lipidol. 5(5), 414-417 (2011).