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useful for immunohistochemical staining to demonstrate the localization of CML in some pathological tissues.

Anti CML [Nε-(carboxymethyl)lysine] Monoclonal Antibody Advanced Glycation End[AGE] Products

Background

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 (AGE). Recent immunological studies using anti-AGE antibody (6D12) demonstrated the presence of AGE-modified proteins in several human tissues.
(1) human lens (nondiabetic and noncataractous)
(2) renal proximal tubules in patients with diabetic nephropathy and chronic renal failure
(3) diabetic retina
(4) peripheral nerves of diabetic neuropathy
(5) atherosclerotic lesions of arterial walls
(6) β2-microglobulin forming amyloid fibrils in patients with hemodialysis-related amyloidosis
(7) senile plaques of patients with Alzheimer’s disease
(8) the peritoneum of CAPD patients
(9) skin elastin in actinic elastosis
(10) ceriod/lipofuscin deposits
These results suggest a potential role of AGE-modification in normal aging as well as age-enhanced disease processes. This antibody named as 6D12 has been used to demonstrate AGE-modified proteins in these human tissues, indicating potential usefulness of this antibody for histochemical identification and biochemical quantification of AGE-modified proteins.

 

Nε-(carboxymethyl)lysine (CML) is a major antigenic AGE 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. NF1G is monoclonal antibody specific for CML and useful for immunohistochemical staining to demonstrate the localization of CML in some pathological tissues.


 AGEs Antibody Flyer [PDF]
 AGEs Antibody Flyer (print file) [PDF]
 

 

Positive observation Human aorta atherosclerotic lesion
(Usage concentration 3g/mL)

Anti-CML monoclonal antibody(NF-1G) has ten times better sensibility than a former Anti-CML monoclonal antibody(CMS-10).
This antibody is a monoclonal that very specific to CML and don’t recognize CEL and very useful for localyzed analysis in immunohistochemistry.

Package Size 50µg  (200µL/vial)
Format
Buffer
Mouse monoclonal antibody 0.25 mg/mL
Block Ace as a stabilizer, containing 0.1% Proclin as a bacteriostat
Storage Store below  -20°C.
Once thawed, store at 4°C. Repeated freeze-thaw cycles should be avoided.
Clone No. NF-1G
Subclass IgG2a
Purification method The splenic lymphocytes from BALB/c mouse, immunized with CML-HSA were fused to myeloma P3U1 cells. The cell line (NF1G) with positive reaction was grown in ascitic fluid of BALB/c mouse, from which the antibody was purified by Protein G affinity chromatography.
Working dilution for immunohistochemistry: 5-10µg/mL;
for ELISA: 0.1-1.0µg/mL

Anti-CML monoclonal antibody(NF-1G) has a ten times better sensibility than a formerAnti-CML monoclonal antibody(CMS-10). Please select the clone according to the purpose of the experiment.

Product List

Product Name Cat# Quantity Price

Anti CML

KAL-KH024 50UG

¥ 55,000
$ 734
€ 550

Anti CML

KAL-KH024-01 50UG

¥ 70,000
$ 934
€ 700

Anti CML

KAL-KH024-02 50UG

¥ 70,000
$ 934
€ 700

Citation
  • Specific ion channels contribute to key elements of pathology during secondary degeneration following neurotrauma.
    O'Hare Doig RL, Chiha W, Giacci MK, Yates NJ, Bartlett CA, Smith NM, Hodgetts SI, Harvey AR, Fitzgerald M.
    BMC Neurosci. 2017 Aug 14;18(1):62. PMID: 28806920
  • Diabetes-induced alterations in tissue collagen and carboxymethyllysine in rat kidneys: Association with increased collagen-degrading proteinases and amelioration by Cu(II)-selective chelation.
    Brings S, Zhang S, Choong YS, Hogl S, Middleditch M, Kamalov M, Brimble MA, Gong D, Cooper GJ.
    Biochim Biophys Acta. 2015 Aug;1852(8):1610-8. PMID: 25900786
  • AGEs-RAGE mediated up-regulation of connexin43 in activated human microglial CHME-5 cells.
    Shaikh SB, Uy B, Perera A, Nicholson LF.
    Neurochem Int. 2012 May;60(6):640-51. PMID: 22417726

References
  • The advanced glycation end product, Nepsilon-(carboxymethyl)lysine, is a product of both lipid peroxidation and glycoxidation reactions.
    Fu MX, Requena JR, Jenkins AJ, Lyons TJ, Baynes JW, Thorpe SR.
    J Biol Chem. 1996 Apr 26;271(17):9982-6. PMID: 8626637
  • Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications.
    McLellan AC, Thornalley PJ, Benn J, Sonksen PH.
    Clin Sci (Lond). 1994 Jul;87(1):21-9. PMID: 8062515
  • Oxidation of glycated proteins: age-dependent accumulation of N epsilon-(carboxymethyl)lysine in lens proteins.
    Dunn JA, Patrick JS, Thorpe SR, Baynes JW.
    Biochemistry. 1989 Nov 28;28(24):9464-8. PMID: 2514802

To be used for research only. DO NOT use for human gene therapy or clinical diagnosis.