Concentration:	0.20 mg/ml (vortex before apply for gel electrophoresis)
Size:	100 μl (20 applications of 5 μl each). ApoCs 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 6.6 kDa for apoCI, 8.5 kDa for apoCII, and 8.7 kDa for ApoCIII; ApoAII appears as weak visible band between ApoCI and ApoCII.
Source:	From purified ApoCs and ApoAII; 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 ApoCs Standard allows you to check the result of your gel run and to judge western transfer efficiency. The attached gel 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.

 

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

 

Importance

ApoCI contains 57 amino acid residues and the m.w. is 6.6 kDa (Jackson et al., 1974). ApoCI has been found to activate LCAT (Liu and Subbaiah 1993).

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).

ApoCIII contains 79 amino acid residues. The m.w. is 8.7 kDa (Brewer et al., 1974). 

Jackson R.L., J. T. Sparrow, H. N. Baker, J.D. Morrisett, O. D. Taunton, and A. M. Jr. Gotto. “The primary structure of apolipoprotein-serine.” J. Biol. Chem. 249.16 (1974): 5308-13.

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.

Brewer, H. B., R. Shulman, P. Herbert, R. Ronan, and K. Wehrly. “The complete amino acid sequence of alanine apolipoprotein (apoC-3), and apolipoprotein from human plasma very low density lipoproteins.” J Biol Chem 249.15 (1974):4975-84.

 

Citations

[SP4]

2016

Koska, Juraj; Yassine, Hussein; Trenchevska, Olgica; Sinari, Shripad; Schwenke, Dawn C.; Yen, Frances T. et al. (2016): Disialylated apolipoprotein C-III proteoform is associated with improved lipids in prediabetes and type 2 diabetes. In Journal of lipid research 57 (5), pp. 894–905. DOI: 10.1194/jlr.P064816.

academy biomed[A05]绵羊抗人类载脂蛋白AII多克隆抗体12A-S1a学院生物医学公司$ 155.00$ 155.00目录号数量1寄主物种： 羊浓度： 1毫克/毫升（OD 1.35 / 280 nm）抗原： 人类载脂蛋白AII纯化： 亲和纯化缓冲： 75 mM磷酸钠，75 mM NaCl，0.5 mM EDTA，0.02％NaN3，pH 7.2特异性 与人载脂蛋白AII特异性结合。免疫印迹和ELISA的稀释范围：1,000至80,000。用： 该抗体可用于检测血浆和脂蛋白中的载脂蛋白AII，免疫测定，免疫印迹，酶结合或生物素化。存储： -20°C长期保存，4°C短期保存。等分试样，以避免反复冻结和解冻。 *这些产品仅用于研究或制造用途，不能用于人体治疗或诊断应用。 重要性Apo AII占HDL的25％。它在人血浆中以77条氨基酸残基的2条相同链的二聚体形式存在，并通过二硫键连接。据报道，单链的分子量为8.7kDa（Brewer等，1972）。对小鼠的研究报道，apoAII可能具有促动脉粥样硬化作用（Warden等，1993）。然而，一项大型的欧洲前瞻性研究中的病例对照研究表明，血浆Apo AII浓度与冠心病事件密切相关（Birjmohun等，2007）。Birjmohun，RS，GM Dallinga-Thie，JA Kuivenhoven，ESg Stroes，JD Otvos，NJ Wareham，R.Luben，JJp Kastelein，K.-T. Khaw和SM Boekholdt。“载脂蛋白A-II与未来冠状动脉疾病的风险成反比。” 循环116（2007）：2029-035。Brewer，HB，SE Lux，R.Ronan和KM John。“人ApoLp-Gln-II（apoA-II），一种从高密度脂蛋白复合物中分离的载脂蛋白的氨基酸序列。” 美国国家科学院院刊69.5（1972）：1304-308。Warden，C.，C.Hedrick，J.Qiao，L.Castellani和A.Lusis。“过表达载脂蛋白A-II的转基因小鼠中的动脉粥样硬化。” 科学261（1993）：469-72。