Product name : Anti CML Monoclonal Antibody (Clone:CMS-10)
Catalog number : 302-08831
Supplier name : BBridge
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Anti CML Monoclonal Antibody (Clone:CMS-10) http://biotech-map.com/aa_search/table_sample.html?q=monoclonal&filter=
Anti CML Monoclonal Antibody (Clone:CMS-10) is a monoclonal antibody which is greatly purified and with high binding affinity for the antigen that it is risen against. If used correctly and according the protocol, this antibody will provide excellent and reproducible results with guaranteed success for the tested and confirmed applications. Amongst the advantages of the monoclonal antibodies are: the fact that while the hybridoma takes a bit longer to be produced, once the line is ready there is virtually an endless supply of these antibodie throughout time with little to no variations in recognition sites of the antigen in different batches; in comparison to the polyclonal antibodies monoclonal antibodies are highly specific to a given epitope and can be used in applications where specific targeting is required.
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: human lens (nondiabetic and noncataractous), renal proximal tubules in patients with diabetic nephropathy and chronic renal failure, diabetic retina,
peripheral nerves of diabetic neuropathy, atherosclerotic lesions of arterial walls, 2-microglobulin forming amyloid fibrils in patients with hemodialysis-related amyloidosis, senile plaques of patients with Alzheimer’s disease, the peritoneum of CAPD patients, skin elastin in actinic elastosis, and 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.
N-(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.
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