[A11] Rabbit Anti-Human Apolipoprotein CII Polyclonal Antibody

[A11] Rabbit Anti-Human Apolipoprotein CII Polyclonal Antibody

32A-R1a

Academy Bio-Medical Company, Inc.

  • $295.00


Host Species: Rabbit
Concentration: 1 mg/ml (OD 1.35 / 280 nm)
Antigen: Human Apolipoprotein CII
Purification: Affinity purified
Buffer: 75 mM Sodium Phosphate, 75 mM NaCl, 0.5 mM EDTA, 0.02% NaN3, pH 7.2
Specificity Specifically binds to human apo CII. Dilution for immunoblot and ELISA range: 1,000 to 8,000.
Use: The antibody can be used for detection of apo CII in plasma and lipoproteins, immunoassays, immunoblots, enzyme conjugation, or biotinylation.
Storage: -20°C for long-term storage, 4°C for short- term storage. Aliquot to avoid repeated freezing and thawing.

 

*These products are for research or manufacturing use only, not for use in human therapeutic or diagnostic applications.

 

Importance

ApoCII contains 78 amino acid residues. The m.w. is 8.5 kDa (Jackson et al., 1977). The lipid-binding domain of Apo CII is localized to a region in the N-terminal with a strongly amphipathic nature (Macphee et al., 1999).

Apo CII is also one of the key components of the metabolism of total triacylglycerol-rich lipoproteins by activating lipoprotein lipase that hydrolyzes fatty acids from triacylglycerols in chylomicrons (Kei et al., 2012).

Jackson, R. L., h. N. Baker, E. B. Gilliam, and A. M. Jr. Gotto. “Primary structure of very low density apolipoprotein C-II of human plasma.” Proc Natl. Acad. Sci. USA 74.5 (1977): 1942-5.

Kei, Anastazia A., Theodosios D. Filippatos, Vasilios Tsimihodimos, and Moses S. Elisaf. "A Review of the Role of Apolipoprotein C-II in Lipoprotein Metabolism and Cardiovascular Disease." Metabolism 61.7 (2012): 906-21.

Macphee, Cait E., Geoffrey J. Howlett, William H. Sawyer, and Andrew H. A. Clayton. "Helix−Helix Association of a Lipid-Bound Amphipathic α-Helix Derived from Apolipoprotein C-II." Biochemistry 38.33 (1999): 10878-0884.

 

Citations

[A10][A11] 2017 Wassef, Hanny; Bissonnette, Simon; Dufour, Robert; Davignon, Jean; Faraj, May (2017): Enrichment of Triglyceride-Rich Lipoproteins with Apolipoprotein C-I Is Positively Associated with Their Delayed Plasma Clearance Independently of Other Transferable Apolipoproteins in Postmenopausal Overweight and Obese Women. In J. Nutr. 147 (5), pp. 754–762. DOI: 10.3945/jn.116.242750.
[A10][A11] 2015 Trenchevska, Olgica; Schaab, Matthew R.; Nelson, Randall W.; Nedelkov, Dobrin (2015): Development of multiplex mass spectrometric immunoassay for detection and quantification of apolipoproteins C-I, C-II, C-III and their proteoforms. In Methods (San Diego, Calif.) 81, pp. 86–92. DOI: 10.1016/j.ymeth.2015.02.020.
[A10][A11] 2015 Yassine, Hussein N.; Trenchevska, Olgica; Ramrakhiani, Ambika; Parekh, Aarushi; Koska, Juraj; Walker, Ryan W. et al. (2015): The Association of Human Apolipoprotein C-III Sialylation Proteoforms with Plasma Triglycerides. In PLoS ONE 10 (12), e0144138. DOI: 10.1371/journal.pone.0144138.
[A10][A11] 2006 Kawakami, Akio; Aikawa, Masanori; Libby, Peter; Alcaide, Pilar; Luscinskas, Francis W.; Sacks, Frank M. (2006): Apolipoprotein CIII in apolipoprotein B lipoproteins enhances the adhesion of human monocytic cells to endothelial cells. In Circulation 113 (5), pp. 691–700. DOI: 10.1161/CIRCULATIONAHA.105.591743.
[A10][A11] 2005 Nedelkov, Dobrin; Kiernan, Urban A.; Niederkofler, Eric E.; Tubbs, Kemmons A.; Nelson, Randall W. (2005): Investigating diversity in human plasma proteins. In Proc Natl Acad Sci USA 102 (31), pp. 10852–10857. DOI: 10.1073/pnas.0500426102.
[A10][A11] 2001 Deeg, M. A.; Bierman, E. L.; Cheung, M. C. (2001): GPI-specific phospholipase D associates with an apoA-I- and apoA-IV-containing complex. In J. Lipid Res. 42 (3), pp. 442–451.

 


We Also Recommend