[H03] HRP-conjugated Goat Anti-Human Apolipoprotein AI11H-G1a
|Concentration:||1 mg/ml (OD 1.35 / 280 nm)|
|Antigen:||Human Apolipoprotein AI|
|Buffer:||50 mM PBS, 0.1 M NaCl, and 0.01% Thiomersal, pH 7.4.|
|Specificity||Specifically binds to human apo AI. Dilution for immunoblot and ELISA range: 1,000 to 8,000.|
|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.|
|Form:||Freeze dried powder|
|Stabilizer:||10 mg / ml Bovine Serum Albumin.|
Freeze-dried product should be stored refrigerated until opened. After opening, restore to suggested ml volume with distilled water. If it is not completely clear after standing for 1-2 hours at room temperature, centrifuge the product. It is stable for several weeks at 4°C as an undiluted liquid. Do not use for more than one day after dilution. For extended storage after reconstitution, we suggest aliquot to avoid repeated freezing and thawing; or the addition of an equal volume of glycerol to make a final glycerol concentration of 50%, followed by storage at -20°C. The concentration of protein and buffer salts will decrease to one-half of the original after the addition of glycerol.
*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.
|[H03]||2020||Amaya-Montoya, Mateo; Pinzón-Cortés, Jairo A.; Silva-Bermúdez, Lina S.; Ruiz-Manco, Daniel; Pérez-Matos, Maria C.; Jiménez-Mora, Mario A.; Mendivil, Carlos O. (2020): ApoE and apoC-III-defined HDL subtypes: a descriptive study of their lecithin cholesterol acyl transferase and cholesteryl ester transfer protein content and activity. Lipids Health Dis 19 (1), p. 106. DOI: 10.1186/s12944-020-01291-x.
|[H03]||2020||Koch, Manja; DeKosky, Steven T.; Goodman, Matthew; Sun, Jiehuan; Furtado, Jeremy D.; Fitzpatrick, Annette L. et al. (2020): High density lipoprotein and its apolipoprotein-defined subspecies and risk of dementia. In J. Lipid Res. 61 (3), pp. 445–454. DOI: 10.1194/jlr.P119000473.
|[H03]||2018||Aroner, Sarah A.; Koch, Manja; Mukamal, Kenneth J.; Furtado, Jeremy D.; Stein, James H.; Tattersall, Matthew C. et al. (2018): High‐Density Lipoprotein Subspecies Defined by Apolipoprotein C‐III and Subclinical Atherosclerosis Measures: MESA (The Multi‐Ethnic Study of Atherosclerosis). In Journal of the American Heart Association 7 (6), p. 40. DOI: 10.1161/JAHA.117.007824.|
|[H03]||2018||Furtado, Jeremy D.; Yamamoto, Rain; Melchior, John T.; Andraski, Allison B.; Gamez-Guerrero, Maria; Mulcahy, Patrick et al. (2018): Distinct Proteomic Signatures in 16 HDL (High-Density Lipoprotein) Subspecies. In Arterioscler Thromb Vasc Biol. 38 (12), pp. 2827–2842. DOI: 10.1161/ATVBAHA.118.311607.|
|[H03]||2017||Koch, Manja; Furtado, Jeremy D.; Jiang, Gordon Z.; Gray, Brianna E.; Cai, Tianxi; Sacks, Frank et al. (2017): Associations of anthropometry and lifestyle factors with HDL subspecies according to apolipoprotein C-III. In Journal of Lipid Research 58 (6), pp. 1196–1203. DOI: 10.1194/jlr.P073288.|
|[H03]||2011||Wang, Yanan; Berbée, Jimmy F. P.; Stroes, Erik S.; Smit, Johannes W. A.; Havekes, Louis M.; Romijn, Johannes A.; Rensen, Patrick C. N. (2011): CETP expression reverses the reconstituted HDL-induced increase in VLDL. In J. Lipid Res. 52 (8), pp. 1533–1541. DOI: 10.1194/jlr.M016659.|
|[H03]||2009||Gillard, Baiba K.; Lin, Hu-Yu Alice; Massey, John B.; Pownall, Henry J. (2009): Apolipoproteins A-I, A-II and E are independently distributed among intracellular and newly secreted HDL of human hepatoma cells. In Biochimica et Biophysica Acta 1791 (12), pp. 1125–1132. DOI: 10.1016/j.bbalip.2009.07.004.|
|[H03]||2009||Rosales, Corina; Gillard, Baiba K.; Courtney, Harry S.; Blanco-Vaca, Francisco; Pownall, Henry J. (2009): Apolipoprotein Modulation of Streptococcal Serum Opacity Factor Activity against Human Plasma High-Density Lipoproteins. In Biochemistry 48 (33), pp. 8070–8076. DOI: 10.1021/bi901087z.|
|[H03]||2009||Vries-van der Weij, Jitske de; Haan, Willeke de; Hu, Lihui; Kuif, Maarten; Oei, H. Ling D. W.; van der Hoorn, José W. A. et al. (2009): Bexarotene Induces Dyslipidemia by Increased Very Low-Density Lipoprotein Production and Cholesteryl Ester Transfer Protein-Mediated Reduction of High-Density Lipoprotein. In Endocrinology 150 (5), pp. 2368–2375. DOI: 10.1210/en.2008-1540.|
|[H03]||2007||Gillard, Baiba K.; Courtney, Harry S.; Massey, John B.; Pownall, Henry J. (2007): Serum opacity factor unmasks human plasma high-density lipoprotein instability via selective delipidation and apolipoprotein A-I desorption. In Biochemistry 46 (45), pp. 12968–12978. DOI: 10.1021/bi701525w.|
|[H03]||2004||Pastore, Lucio; Belalcazar, L. Maria; Oka, Kazuhiro; Cela, Racel; Lee, Brendan; Chan, Lawrence; Beaudet, Arthur L. (2004): Helper-dependent adenoviral vector-mediated long-term expression of human apolipoprotein A-I reduces atherosclerosis in apo E-deficient mice. In Gene 327 (2), pp. 153–160. DOI: 10.1016/j.gene.2003.11.024.|