Concentration:	1 mg / ml, determined by the Lowry method
Source:	Bovine Serum Albumin was purchased from Boehringer Mannheim and was modified by caboxymethylation to form CML modified BSA.
Buffer:	In 75 mM Sodium Phosphate, 75 m M NaCl, 0.02 % NaN3, 1 mM EDTA, p H 7.4.
Storage:	2 - 8°C for short and -20°C for 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

The initial step in AGE formation is the nonenzymatic attachment of sugar aldehydes or ketones to the side chains of lysine, arginine, and possibly histidine (Vlassara et al., 1994). The lysine ε-amino-derived glycation product, or Schiff base, rearranges to form a more stable amino ketone intermediate known as the Amadori product. The presence of the Amadori product (Nagai et al., 1997), indicative of active glycation, can be demonstrated by its reduction to a stable epimeric mixture of 1-glycitol-lysine and 1-mannitol-lysine, known collectively as hexitol-lysine (HL).

Immunocytochemical and biochemical studies have suggested that one particular AGE, Nε-(Carboxymethyl)lysine (CML) is the major AGE that accumulates in vivo. Elevated serum levels of CML are detected in patients with diabetes mellitus (Schleicher et al., 1997) and CML is increased in the vascular tissues of diabetic rodents and humans (Meng et al., 1998).

Vlassara H, Bucala R, Striker L. Pathogenic effects of advanced glycosylation: biochemical, biologic, and clinical implications for diabetes and aging. Lab Invest. 1994 Feb;70(2):138-51

Nagai R, Ikeda K, Higashi T, Sano H, Jinnouchi Y, Araki T, Horiuchi S. Hydroxyl radical mediates N epsilon-(carboxymethyl)lysine formation from Amadori product. Biochem Biophys Res Commun. 1997 May 8;234(1):167-72.

Schleicher E.D., E. Wagner and A.G. Nerlich, Increased accumulation of the glycoxidation product N-(carboxymethyl)lysine in human tissues in diabetes and aging. J. Clin. Invest. 99 (1997), pp. 457¯468.

Meng J, Sakata N, Takebayashi S, Asano T, Futata T, Nagai R, Ikeda K, Horiuchi S, Myint T, Taniguchi N. Glycoxidation in aortic collagen from STZ-induced diabetic rats and its relevance to vascular damage. Atherosclerosis. 1998 Feb;136(2):355-65.

 

Citations

[P26]	2018	Klont, Frank; Hadderingh, Marrit; Horvatovich, Péter; Hacken, Nick H. T. ten; Bischoff, Rainer (2018): Affimers as an Alternative to Antibodies in an Affinity LC–MS Assay for Quantification of the Soluble Receptor of Advanced Glycation End-Products (sRAGE) in Human Serum. In J. Proteome Res. 17 (8), pp. 2892–2899. DOI: 10.1021/acs.jproteome.8b00414.
[P26]	2018	Klont, Frank; Pouwels, Simon D.; Hermans, Jos; van de Merbel, Nico C.; Horvatovich, Péter; Hacken, Nick H. T. ten; Bischoff, Rainer (2018): A fully validated liquid chromatography-mass spectrometry method for the quantification of the soluble receptor of advanced glycation end-products (sRAGE) in serum using immunopurification in a 96-well plate format. In Talanta 182, pp. 414–421. DOI: 10.1016/j.talanta.2018.02.015.
[P26]	2017	Grönwall, Caroline; Amara, Khaled; Hardt, Uta; Krishnamurthy, Akilan; Steen, Johanna; Engström, Marianne et al. (2017): Autoreactivity to malondialdehyde-modifications in rheumatoid arthritis is linked to disease activity and synovial pathogenesis. In Journal of autoimmunity 84, pp. 29–45. DOI: 10.1016/j.jaut.2017.06.004.
[P26]	2015	Nedić, Olgica; Rogowska-Wrzesinska, Adelina; Rattan, Suresh I.S. (2015): Standardization and quality control in quantifying non-enzymatic oxidative protein modifications in relation to ageing and disease: Why is it important and why is it hard? In Redox Biology 5, pp. 91–100. DOI: 10.1016/j.redox.2015.04.001.
[P26]	2014	Rogowska-Wrzesinska, A.; Wojdyla, K.; Nedić, O.; Baron, C. P.; Griffiths, H. R. (2014): Analysis of protein carbonylation — pitfalls and promise in commonly used methods. In Free radical research 48 (10), pp. 1145–1162. DOI: 10.3109/10715762.2014.944868.

 

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。