| Concentration: | 0.20 mg/ml (vortex before apply for gel electrophoresis) |
| Size: | 100 μl (20 applications of 5 μl each). ApoB-100 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 ApoB-100 resolves into bands with 515 kDa. |
Source: | From purified Low Density Lipoprotein; 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 ApoB-100 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 (ApoB-100) and lane 2 (Std Mix1) on an Invitrogen 4-20% 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
ApoB exists in human plasma in two isoforms, ApoB-48 (Chen et al., 1987) and Apo B-100 (Wei et al., 1985, Yang et al., 1986a; 1989a,b; 1990; Chen et al., 1986; Yang et al., 1990, Yang and Pownall, 1992). Apo B-100 is the major physiological ligand for the LDL receptor. Apo B-100 is a large monomeric protein, containing 4536 amino acids (m.w. 515 kDa, Yang et al., 1986b).Apo B-100 is synthesized in the liver and is required for the assembly of VLDL. It is found in LDL and VLDL after the removal of the Apo A, E and C. Apo B-48 is present in chylomicrons and their remnants. It is essential for the intestinal absorption of dietary lipids. Apo B levels correlate with the risk of coronary disease.The Apo B protein is directly involved in the retention of LDL with the arterial wall (Olofsson and Boren, 2012). Apo B-48 is synthesized in the small intestine. It comprises approximately half of the N-terminal region of ApoB-100 and is the result of posttranscriptional mRNA editing by a stop codon in the intestine not found in the liver.Chen, S., G. Habib, C. Yang, Z. Gu, B. Lee, S. Weng, S. Cai, J. Deslypere, M. Rosseneu, and Al. Et. "Apolipoprotein B-48 Is the Product of a Messenger RNA with an Organ-specific In-frame Stop Codon." Science 238 (1987): 363- 66.Olofsson, S.-O., and J. Boren. "Apolipoprotein B Secretory Regulation by Degradation." Arteriosclerosis, Thrombosis, and Vascular Biology 32 (2012): 1334-338.Wei, C. F., S. H. Chen, C. Y. Yang, Y. L. Marcel, R. W. Milne, W. H. Li, J. T. Sparrow, A. M. Gotto, and L. Chan. "Molecular Cloning and Expression of Partial cDNAs and Deduced Amino Acid Sequence of a Carboxyl-terminal Fragment of Human Apolipoprotein B-100." Proceedings of the National Academy of Sciences 82 (1985): 7265- 269.Yang, Chao-Yuh, and Pownall, H.J. "In Structure and Function of Plasma Apolipoproteins." Structure and Function of Apolipoproteins. Boca Raton, Fla.: CRC, 1992.Yang, Chao-Yuh, T. W. Kim, S. A. Weng, B. R. Lee, M. L. Yang, and A. M. Gotto. "Isolation and Characterization of Sulfhydryl and Disulfide Peptides of Human Apolipoprotein B-100." Proceedings of the National Academy of Sciences 87 (1990): 5523-527.Yang, Chao-Yuh, Z. W. Gu, S. A. Weng, T. W. Kim, S. H. Chen, H. J. Pownall, P. M. Sharp, S. W. Liu, W. H. Li, and A. M. Gotto. "Structure of Apolipoprotein B-100 of Human Low Density Lipoproteins." Arteriosclerosis, Thrombosis, and Vascular Biology 9 (1989a): 96-108.Yang, Chao-Yuh, Zi-Wei Gu, Lawrence Chan, Henry J. Pownall, and Antonio M. Gotto. "Structure and Functional Domains of Human Apolipoprotein B-100: A Strategy to Elucidate the Structure Information of a Large Protein." Methods in Protein Sequence Analysis (1989b): 466-74.Yang, Chao-Yuh, San-Hwan Chen, Sandra H. Gianturco, William A. Bradley, James T. Sparrow, Masako Tanimura, Wen-Hsiung Li, Doris A. Sparrow, Hans Deloof, Maryvonne Rosseneu, Fu-Shin Lee, Zi-Wei Gu, Antonio M. Gotto, and Lawrence Chan. "Sequence, Structure, Receptor-binding Domains and Internal Repeats of Human Apolipoprotein B-100." Nature 323 (1986a): 738-42.
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。
