![美国生物医学学会/[SP7]人载脂蛋白混合物2 SDS-PAGE标准/146](https://www.ebiomall.cn/images/academybiomed/sp7_300x300.png)
| Concentration: | 0.20 mg/ml (vortex before apply for gel electrophoresis) |
| Size: | 100 μl (20 applications of 5 μl each). Apolipoprotein mix1 Standard is a ready-to-use format - no mixing, heating or reducing required. It is pre-reduced and contains reducing reagents in the loading buffer. The protein standards resolve into bands with ApoCI (MWt. 6.6 kDa), ApoCIII (MWt. 8.7 kDa), ApoAI (MWt. 28 kDa), ApoE (MWt. 37 kDa) and Standard MWt. at 94, 67, 43, 30, 20.1, and 14.4 kDa. |
Source: | From purified Apoproteins; fresh human plasma that has tested negative for Hepatitis C, HIV-I and HIV-II antibodies as well as Hepatitis surface antigens. |
Use: | The Un-Stained Apolipoprotein mix2 Standard allows you to check the result of your gel run and to judge western transfer efficiency. The attached gel A was running with 4 µl of each for lane 1 (ApoB-100) and lane 2 (Std Mix2) on an Invitrogen 4-20% SDS-Gel; while gel B was running with 4 µl of each for lane 1 (ApoCs) and lane 2 (Std Mix2) on an Invitrogen 18% SDS-Gel. |
Buffer: | In loading buffer consists of Tris-HCl, MeSH, SDS, glycerol, and bromophenol. |
Storage: | -20°C for short and long-term storage. Aliquot to avoid repeated freezing and thawing. |
*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.
Citations
| [SP7] | 2018 | Chang, Chiz-Tzung; Shen, Ming-Yi; Hsieh, Ju-Yi; Chang, Chia-Ming; Liao, Hsin-Yi; Chen, Fang-Yu et al. (2018): Increased electronegativity of high-density lipoprotein in uremia patients impairs its functional properties and is associated with the risk of coronary artery disease. In Atherosclerosis 278, pp. 147–155. DOI: 10.1016/j.atherosclerosis.2018.09.009. |
| [SP7] | 2016 | Chang, Chiz-Tzung; Wang, Guei-Jane; Kuo, Chin-Chi; Hsieh, Ju-Yi; Lee, An-Sean; Chang, Chia-Ming et al. (2016): Electronegative Low-density Lipoprotein Increases Coronary Artery Disease Risk in Uremia Patients on Maintenance Hemodialysis. In Medicine 95 (2), e2265. DOI: 10.1097/MD.0000000000002265. |
| [SP7] | 2013 | Hsieh, Ju-Yi; Chang, Chiz-Tzung; Huang, Max T.; Chang, Chia-Ming; Chen, Chia-Ying; Shen, Ming-Yi et al. (2013): Biochemical and Functional Characterization of Charge-Defined Subfractions of High-Density Lipoprotein From Normal Adults. In Anal. Chem. 85 (23), pp. 11440–11448. DOI: 10.1021/ac402516u. |
