Proteins and Peptides - CML001-P1: HSA-CML

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CML001-P1: HSA-CML

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Price: 160 € / 1.8 mg

Control Peptide

Origin:	Human

Format:	liquid conc.

Quantity:	1.8 mg

Concentration:	18 mg/ml

Working concentration:	1-100 µg/ml

Presentation:	Protein solution (HSA-CML) dialysed against PBS, 0.08% NaN3** added

Immunogen:	Human Serum albumin (HSA) synthetically modified at Lysine residues and converted to HSA-N(epsilon)-(Carboxymethyl)-Lysine

Specificity:	CML-HSA will be bound by most polyclonal AGE-antibodies and CML-specific monoclonal antibodies.

Species Specificity:	not relevant

General Information:	Long-term incubation of proteins with glucose leads, through Schiff's base and Amadori rearrangement products, to the formation of advanced glycation end products (AGE) which are characterized by fluorescence, brown color and inter- and intra-molecular cross-linking. Recent immunological studies using anti-AGE antibodies demonstrated the presence of AGE in (i) human lens, (ii) renal proximal tubules in patients with diabetic nephropathy and chronic renal failure, (iii) atherosclerotic lesions of arterial walls, (iv) ß2-microglobulin of carpal tunnel amyloid fibril deposits in patients with hemodialysis-related amyloidosis and (v) brain tissues of patients with Alzheimer's disease. N-epsilon-(carboxymethyl)-lysine was identified to be a major structure in AGE (Dunn et al., 1989). Oxidative cleavage of Amadori-products seems to be the main pathway of CML-formation in vivo. More recent investigations however have shown, that as well lipid-peroxidation as glycoxidation can be involved in CML-build up in vivo (Fu et al., 1996).

Special properties:	PAGE (5-50 µg/lane), western blot, ELISA, antibody pre-absorption for negative control

Applications:	IHC control, ELISA, WB, PAGE,

Storage:	-20°C

References:
1. Kilhovd B.K., Giardino I., Torjesen P.A., Birkeland K.I., Berg, T.J., Thornally P.J., Brownlee M., and Hanssen K.F. (2003) Increased serum levels of the specific AGE-compound methylglyoxal-derived hydroimmidazolone in patiens with type 2 diabetes. Metabolism 52(2); 163-167.

2. Cellek S., Qu W., Schmidt A.M., and Moncada S. (2004) Synergistic action of advanced glycation end products and endogenous nitric oxide leads to neuronal apoptosis in vitro: a new insight into selective nitrergic neuropathy in diabetes. Diabetologia 47(2); 331-339.

Notes:
*BIOLOGO products are intended for in vitro research use only. They must not be used for clinical diagnostics and not for in vivo experiments in humans or animals.