[P26] Carboxymethyl-lysine modified Bovine Serum Albumin (CML-BSA)30P-CML-BS102
|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.
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.
|[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.|