ADMA – high sensitive
Enzyme Immunoassay for the Quantitative Determination of Asymmetric Dimethylarginine (ADMA) in Serum or Plasma of Mice, Rats and in Cell Culture Media
Characteristics
Lower limit of detection: 0.01 µmol/l
Suitable for small sample volumes (5-20 µl).
Samples can be run directly in the assay without any filtration
High precision is guaranteed by over night incubation
Detailed testing in RPMI and DMEM cell culture medium
No cooling procedure during the transportation
No cross reactivity with L-Arginine, SDMA and N-Monomethylarginine
No cross reactivity with drugs
Excellent correlation with LC-MS/MS analysis
Kits with long expiry date (up to 21 month) are in stock ready for shipment
The vascular endothelium plays a central role in the regulation of vascular structure and function, mainly due to the formation of endothelium-derived nitric oxide (NO). NO has been named an “endogenous anti-atherogenic molecule” due to its diverse regulatory functions in vascular homeostasis.
NO is formed by the enzyme NO synthetase (NOS) from the amino acid precursor L-arginine. NOS activity can be downregulated by asymmetric dimethylarginine (ADMA), an endogenous inhibitor of NOS.
The effects of ADMA on NO synthesis and NO-mediated pathophysiological processes have been described in numerous experimental studies. Moreover, elevated ADMA levels in plasma have been found in clinical studies including patients with hypercholesterolemia, hypertension, chronic heart failure, chronic renal failure and other internal disorders.
Recent prospective and cross-sectional studies indicated that elevated ADMA levels are a risk factor for future cardiovascular events and total mortality. ADMA may have diagnostic relevance as a novel cardiovascular risk marker.
The new competitive ADMA – high sensitive – ELISA uses the microtiter plate format. ADMA is bound to the solid phase of the microtiter plate. ADMA in the samples is acylated and competes with solid phase bound ADMA for a fixed number of rabbit anti-ADMA antiserum binding sites. When the system is in equilibrium, free antigen and free antigenantiserum complexes are removed by washing. The antibody bound to the solid phase ADMA is detected by anti-rabbit/peroxidase. The substrate TMB / peroxidase reaction is monitored at 450 nm. The amount of antibody bound to the solid phase ADMA is inversely proportional to the ADMA concentration of the sample.
- Bode-Böger S.M., Scalera F., Kielstein J.T., Martens-Lobenhoffer J., Breithardt G., Fobker M., Reinecke H. Symmetrical Dimethylarginine: A new combined parameter for renal function and extent of coronary artery disease J. Am. Soc. Nephrol. (2006) 17: 1128-1134
- Kielstein J.T., Salpeter S.R.; Bode-Böger S.M., Cooke J.P., Fliser D. Symmetric dimethylarginine (SDMA) as endogenous marker of renal function – a meta-analysis
Nephrol. Dial. Transplant (2006) 21: 2446 – 2451 - Wanby P., Teerlink T., Brudin L., Brattström L., Nilsson I., Palmqvist P., Carlsson M.
Asymmetric dimethylarginine (ADMA) as a risk marker for stroke and TIA in a Swedish population Atherosclerosis (2006) 185: 271 – 277