Antibody Products

Product NameAnti CEL Monoclonal Antibody ( Clone No. KNH-30 ) Peroxidase conjugated

Cat. No.：
KH025-02
sample

Volume： 50μg/200μL
Price： inquiry
Data Sheet Data Sheet
Antigen： CEL-BSA
GenBank ID： –
Immunizing animal： mouse
Purification： ProteinG
Antibody subclass： IgG1
Application ELISA(0.1-1.0μg/mL) Immuno HistoChemistry(5.0-10.0μg/mL)
Cross React Human Mouse Rat Other
Others 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.
CEL is known to generate from protein modification by methylglyoxal . Mclellan et al. demonstrated that plasma methylglyoxal, which is believed to be generate from Embden-Meyerhof and polyol pathways, concentrations in insulin-dependent diabetic patients were about 7-times higher than those of normal individuals. For examples, CEL was identified in human lens proteins at a concentration similar to that of CML and its accumulation increased with age like CML, indicating that CEL may play an important marker for aging and age-dependent disease such as diabetic complications.
Reference
  • Lab Invest. 2001 Jun;81(6):845-61.
    Immunohistochemical distribution and quantitative biochemical detection of advanced glycation end products in fetal to adult rats and in rats with streptozotocin-induced diabetes.
    Ling X, Nagai R, Sakashita N, Takeya M, Horiuchi S, Takahashi K.

  • Ann N Y Acad Sci. 2008 Apr;1126:328-32.
    Modification of vimentin: a general mechanism of nonenzymatic glycation in human skin.
    Kueper T, Grune T, Muhr GM, Lenz H, Wittern KP, Wenck H, St?b F, Blatt T.

  • J Neurochem. 2006 Oct;99(1):177-85.
    Glial fibrillary acidic protein is a major target of glycoxidative and lipoxidative damage in Pick’s disease.
    Muntan? G, Dalf? E, Mart?nez A, Rey MJ, Avila J, P?rez M, Portero M, Pamplona R, Ayala V, Ferrer I.

  • Acta Neuropathol. 2002 Aug;104(2):171-8.
    Selective formation of certain advanced glycation end products in spinal cord astrocytes of humans and mice with superoxide dismutase-1 mutation.
    Shibata N, Hirano A, Hedley-Whyte ET, Dal Canto MC, Nagai R, Uchida K, Horiuchi S, Kawaguchi M, Yamamoto T, Kobayashi M.

  • Biochimie. 2010 Oct;92(10):1379-86.
    N(?)-(carboxymethyl)lysine linkage to α-synuclein and involvement of advanced glycation end products in α-synuclein deposits in an MPTP-intoxicated mouse model.
    Choi YG, Lim S.

  • Brain Pathol. 2010 May;20(3):598-612.
    Purple sweet potato color alleviates D-galactose-induced brain aging in old mice by promoting survival of neurons via PI3K pathway and inhibiting cytochrome C-mediated apoptosis.
    Lu J, Wu DM, Zheng YL, Hu B, Zhang ZF.
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