Antibody Products

Product NameAnti CML Monoclonal Antibody ( Clone No. CMS-10 ) Peroxidase conjugated

Cat. No.：
KH011-02
sample

Volume： 50μg/200μL
Price： inquiry
Data Sheet Data Sheet
Antigen： CML-KLH
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.
Nε-(carboxymethyl)lysine (CML) was a major AGEs structure identified by Banes et al. in 1989. Oxidative cleavage of Amadori products is considered as a major route to CML formation in vivo. Banes also revealed that CML was directly formed from the reaction between lipidoxidative products and Lysine residue. Thus, CML could become a marker of oxidative stress and long term damage to protein in aging, atherosclerosis, and diabetes.
Reference
  • 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

  • J Biochem. 2004 Dec;136(6):831-7.
    Conventional antibody against Nepsilon-(carboxymethyl)lysine (CML) shows cross-reaction to Nepsilon-(carboxyethyl)lysine (CEL): immunochemical quantification of CML with a specific antibody.
    Koito W, Araki T, Horiuchi S, Nagai R.

  • Cancer Lett. 2005 May 26;222(2):237-45.
    Amino acid transport system L is differently expressed in human normal oral keratinocytes and human oral cancer cells.
    Yoon JH, Kim IJ, Kim H, Kim HJ, Jeong MJ, Ahn SG, Kim SA, Lee CH, Choi BK, Kim JK, Jung KY, Lee S, Kanai Y, Endou H, Kim DK.

  • Biochimie. 2010 Oct;92(10):1379-86.
    N(ɛ)-(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.

  • PLoS One. 2010 Nov 29;5(11):e15062.
    The chaperone-dependent ubiquitin ligase CHIP targets HIF-1α for degradation in the presence of methylglyoxal.
    Bento CF, Fernandes R, Ramalho J, Marques C, Shang F, Taylor A, Pereira P.

  • J Immunol. 2011 Mar 1;186(5):3248-57.
    Septic shock is associated with receptor for advanced glycation end products ligation of LPS.
    Yamamoto Y, Harashima A, Saito H, Tsuneyama K, Munesue S, Motoyoshi S, Han D, Watanabe T, Asano M, Takasawa S, Okamoto H, Shimura S, Karasawa T, Yonekura H, Yamamoto H.
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How to Order

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Cosmo Bio USA, Inc.
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Funakoshi Corporation
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Sceti K.K.
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