[A20] Goat Anti-CML (Carboxymethyl-lysine) Polyclonal Antibody, Academy Bio-medical Company, Inc.

[A20] Goat Anti-CML (Carboxymethyl-lysine) Polyclonal Antibody

CML30A-G1a

Academy Bio-Medical Company, Inc.

  • $281.00


Host Species: Goat
Concentration: 1 mg/ml (OD 1.35 / 280 nm)
Antigen: CML-KLH
Purification: Affinity purified
Buffer: 75 mM Sodium Phosphate, 75 mM NaCl, 0.5 mM EDTA, 0.02% NaN3, pH 7.2
Specificity Specifically binds to CML modified proteins. Dilution for immunoblot and ELISA range: 1,000 to 20,000. (A slight amount of precipitation may have occurred during storage due to the natural properties of these antibodies; please centrifuge before use.).
Use: The antibody can be used for detection of CML in plasma, lipoproteins, and other proteins, immunoassays, immunoblots, enzyme conjugation, or biotinylation.
Storage: -20°C for long-term storage, 4°C for short- 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

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

[A20][A21] 2014 Sáyago-Ayerdi, Sonia G.; Mateos, Raquel; Ortiz-Basurto, Rosa I.; Largo, Carlota; Serrano, José; Granado-Serrano, Ana Belén et al. (2014): Effects of consuming diets containing Agave tequilana dietary fibre and jamaica calyces on body weight gain and redox status in hypercholesterolemic rats. In Food chemistry 148, pp. 54–59. DOI: 10.1016/j.foodchem.2013.10.004.
[A20][A21] 2009 Woltjer, Randall L.; Sonnen, Joshua A.; Sokal, Izabela; Rung, Lisa G.; Yang, Wan; Kjerulf, John D. et al. (2009): Quantitation and Mapping of Cerebral Detergent-Insoluble Proteins in the Elderly. In Brain Pathology 19 (3), pp. 365–374. DOI: 10.1111/j.1750-3639.2008.00190.x.

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