[S03] Goat Anti-Human Apolipoprotein AI Antiserum11S-G2-1.5ml
|Antigen:||Human Apolipoprotein AI|
Specifically binds to human apo AI. Dilution for immunoblot and ELISA range: 1,000 to 400,000. Minor Apo AII and Albumin removed.
|Use:||The antibody can be used for detection of apo AI 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.
Apo AI comprises approximately 70% of the protein moiety in HDL. It is a single polypeptide chain consisting of 243 amino acid residues without disulfide bound and with glutamic acid as the C-terminal residue and aspartic acid as the N-terminal residue. The molecular weight is reported to be 28 kDa (Brewer et al., 1978).
The roles of Apo AI in HDL function include reverse cholesterol transportation, lipid cholesterol binding, lecithin-cholesterol acyl transferase (LCAT) activation, and receptor binding, which is responsible for cholesterol esterification in plasma. Besides participate in cholesterol metabolism, Apo AI and HDL also suppress neutrophil activation, inhibit bacterial endotoxin, induce trypanosomal lysis, and other physiological activities. (Brouillette et al., 2001)
Apo AI levels may be inversely related to the risk of coronary disease. In previous research, Apo AI may affect diet-induced inflammation by either directly or indirectly altering lipid rafts. (Cheng et al., 2012)
Brewer, H. B., T. Fairwell, A. LaRue, R. Ronan, A. Houser, and T. J. Bronzert. “The amino acid sequence of human Apoa-I, an apolipoprotein isolated from high density lipoproteins.” Biochemical and Biophysical Research Communications 80.3 (1978): 623-30.
Brouillette, Christie G., G.m. Anantharamaiah, Jeffrey A. Engler, and David W. Borhani. "Structural Models of Human Apolipoprotein A-I: A Critical Analysis and Review." Biochimica Et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids (2001): 4-46.
Cheng, Andrew M., Priya Handa, Sanshiro Tateya, Jay Schwartz, Chongren Tang, Poulami Mitra, John F. Oram, Alan Chait, and Francis Kim. "Apolipoprotein A-I Attenuates Palmitate-Mediated NF-κB Activation by Reducing Toll-Like Receptor-4 Recruitment into Lipid Rafts." PLoS ONE 7.3 (2012): e33917.
|[S03]||2018||Iqbal, Jahangir; Walsh, Meghan T.; Hammad, Samar M.; Cuchel, Marina; Rader, Daniel J.; Hussain, M. Mahmood (2018): ATP binding cassette family A protein 1 determines hexosylceramide and sphingomyelin levels in human and mouse plasma. In Journal of lipid research 59 (11), pp. 2084–2097. DOI: 10.1194/jlr.M087502.|
|[S03]||2015||Iqbal, Jahangir; Walsh, Meghan T.; Hammad, Samar M.; Cuchel, Marina; Tarugi, Patrizia; Hegele, Robert A. et al. (2015): Microsomal Triglyceride Transfer Protein Transfers and Determines Plasma Concentrations of Ceramide and Sphingomyelin but Not Glycosylceramide. In J. Biol. Chem. 290 (43), pp. 25863–25875. DOI: 10.1074/jbc.M115.659110.|
|[S03]||2007||Vedhachalam, Charulatha; Duong, Phu T.; Nickel, Margaret; Nguyen, David; Dhanasekaran, Padmaja; Saito, Hiroyuki et al. (2007): Mechanism of ATP-binding cassette transporter A1-mediated cellular lipid efflux to apolipoprotein A-I and formation of high density lipoprotein particles. In J. Biol. Chem. 282 (34), pp. 25123–25130. DOI: 10.1074/jbc.M704590200.|
|[S03]||2005||Nakano, Takanari; Nagata, Atsuo (2005): Oxidative susceptibility of apolipoprotein AI in serum. In Clinica Chimica Acta 362 (1-2), pp. 119–124. DOI: 10.1016/j.cccn.2005.06.001.|