[G01] Goat Anti-Human Apolipoprotein AI Sepharose™ 4B Gel, Academy Bio-medical Company, Inc.

[G01] Goat Anti-Human Apolipoprotein AI Sepharose™ 4B Gel

11A-G1 Resin-1ml

Academy Bio-Medical Company, Inc.

  • $1,239.00


Host Species: Goat
Concentration: ≥  5 mg/ml
Source:

Polyclonal goat antibody human apo AI coupled with CNBr-activated Sepharose 4B.

Preservation:

75 mM PBS, 75 mM NaCl, 0.5 mM EDTA, 0.02% NaN3, 0.1mM PMSF, pH 7.3.

Specificity

Specifically binds to human apo AI.

Use:

Affinity purification column.

Storage:

2-8ºC store in buffer with 0.5 mM EDTA and 0.02% NaN3, 0.1 mM PMSF. DO NOT FREEZE!

 

*Sepharose is a trademark of GE Healthcare Life Sciences, Sweden.

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

 

Importance

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.

 

Importance

[G01] 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.
[G01] 2016 Singh, Sasha A.; Andraski, Allison B.; Pieper, Brett; Goh, Wilson; Mendivil, Carlos O.; Sacks, Frank M.; Aikawa, Masanori (2016): Multiple apolipoprotein kinetics measured in human HDL by high-resolution/accurate mass parallel reaction monitoring. In J. Lipid Res. 57 (4), pp. 714–728. DOI: 10.1194/jlr.D061432.
[G01] 2015 Laurent, Louise C.; Abdel-Mageed, Asim B.; Adelson, P. David; Arango, Jorge; Balaj, Leonora; Breakefield, Xandra et al. (2015): Meeting report: discussions and preliminary findings on extracellular RNA measurement methods from laboratories in the NIH Extracellular RNA Communication Consortium. In Journal of Extracellular Vesicles 4 (1), p. 26533. DOI: 10.3402/jev.v4.26533.
[G01] 2014 Tabet, Fatiha; Vickers, Kasey C.; Cuesta Torres, Luisa F.; Wiese, Carrie B.; Shoucri, Bassem M.; Lambert, Gilles et al. (2014): HDL-transferred microRNA-223 regulates ICAM-1 expression in endothelial cells. In Nature communications 5, p. 3292. DOI: 10.1038/ncomms4292.

 


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