Anti-CML, Mouse-Mono (NF-1G) (Cat. No. KH024)

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  • Item #: KH024
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Anti-CML, Mouse-Mono (NF-1G)

Cat. No. KH024

Store at -20°C

Size 50µg

Host Animal- Mouse

Application- ELISA, IHC


Purification- APu

Clone- NF1G

Class- IgG



Reaction of protein amino groups with glucose leads, through the early products such as a Schiff base and Amadori rearrangement products, to the formation of advanced glycation end products (AGEs). Recent immunological studies using anti-AGEs antibody (6D12) demonstrated the presence of AGEs-modified proteins in several human tissues: (ⅰ) human lens (nondiabetic and noncataractous), (ⅱ) renal proximal tubules in patients with diabetic nephropathy and chronic renal failure, (ⅲ) diabetic retina, (ⅳ) peripheral nerves of diabetic neuropathy, (ⅴ) atherosclerotic lesions of arterial walls, (ⅵ)β2-microglobulin forming amyloid fibrils in patients with hemodialysis-related amyloidosis, (ⅶ) senile plaques of patients with Alzheimer’s disease, (ⅷ) the peritoneum of CAPD patients, (ⅸ) skin elastin in actinic elastosis, and (ⅹ) ceriod/lipofuscin deposits. These results suggest a potential role of AGEs-modification in normal aging as well as age-enhanced disease processes. This antibody named as 6D12 has been used to demonstrate AGEs-modified proteins in these human tissues, indicating potential usefulness of this antibody for histochemical identification and biochemical quantification of AGEs-modified proteins. Nε-(carboxymethyl)lysine (CML) is a major antigenic AGEs structure in vivo and is known to be generated from Oxidative cleavage of Amadori product. In addition to amadori product, CML formation also takes place through glyoxal, which is generated from the autoxidation of glucose and unsaturated fatty acids. NF-1G is monoclonal antibody specific for CML and useful for immunohistochemical staining to demonstrate the localization of CML in some pathological tissues.



1. Dunn JA, Patrick JS, Thorpe SR, Baynes JW (1989): Oxidation of glycated proteins: Age-dependent accumulation of Nε-(carboxymethyl) lysine in lens proteins. Biochemistry. 28: 9464-9468.

2. Fu MX, Requena JR, Jenkins AJ, Lions TJ, Baynes JW, Thorpe SR(1996): The advanced glycation end product, Nε-(carboxymethyl) lysine, is a product of both lipid peroxidation and glycoxidation reactions. J.Biol.Chem.271: 9982-9986

3. Mclellan AC, Thornalley PJ, Benn J, Sonksen PH: Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications. Clinical Science 87: 21-29, 1994

These references are the background of CML , and are not this antibody examples .


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