ADMA (Asymmetric Dimethylarginine) / Arginine ELISA Assay Kit

$1,830.00

The Eagle Biosciences ADMA (Asymmetric Dimethylarginine) / Arginine ELISA Assay Kit is intended for the quantitative determination of Endogenous Asymmetric Dimethylarginine (ADMA) and L-Arginine in EDTA-Plasma. The ADMA (Asymmetric Dimethylarginine) / Arginine ELISA Assay Kit is for research use only and not to be used in clinical, therapeutic or diagnostic procedures.

ADMA (Asymmetric Dimethylarginine) / Arginine ELISA Assay Kit

For Research Use Only

Size: 1×96 wells
Sensitivity: ADMA: 0.01 µmol/L, Arginine: 3.0 µmol/L
Dynamic Range: ADMA: 0.1 – 5.0 µmol/L, Arginine: 6-600 µmol/L,
Incubation Time: Overnight
Sample Type: EDTA Plasma
Sample Size: 20 µL

Controls Included

Product Developed and Manufactured in Germany EA207/96


Reference Values for the ADMA Arginine ELISA Assay Kit (Normal)
ADMA     0.4 – 0.75 µmol/l
Arginine   20 – 80 µmol/l
It is suggested that each laboratory establish its own normal ranges.


For a Full Listing of Publications utilizing these ADMA ELISA Assay kits, click on the link below:
ADMA ELISA Assay Kit Publications

Learn more about ADMA at Eagle Biosciences Biomarker Spotlight page dedicated to ADMA here:
ADMA Biomarker Spotlight

Additional Information

Assay Principle


The new competitive ADMA (Asymmetric Dimethylarginine) / Arginine ELISA Assay Kit uses the microtiter plate format. Antigen is bound to the solid phase of the microtiter plate. Antigen in the samples is acylated and competes with solid phase bound antigen for a fixed number of antiserum binding sites. When the system is in equilibrium, free antigen and free antigen-antiserum complexes are removed by washing. The antibody bound to the solid phase ADMA and Arginine, respectively are detected by anti-rabbit/peroxidase. The substrate TMB / peroxidase reaction is monitored at 450 nm. The amount of antibody bound to the solid phase antigen is inversely proportional to the antigen concentration of the sample.

Assay Background


Nitric oxide (NO which is formed in the vascular endothelium plays a crucial role in the regulation of vascular structure and function. 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 synthase (NOS) from the amino acid precursor L-arginine. NOS activity is inhibited 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 and clinical studies, including samples with hyper­cholesterolemia, hypertension, chronic heart failure, chronic renal failure and other internal disorders.  Elevated ADMA levels are a risk factor for future cardiovascular events and total mortality, as evidenced by prospective clinical studies comprising more than 10,000 participants. Thus, studies have shown that ADMA has diagnostic relevance as a novel cardiovascular risk marker.

Importantly, high ADMA levels and low L-arginine/ADMA ratio were both independent predictors of death in the community-based Framingham Offspring Study. As ADMA competes with L-arginine for binding to NO synthase, many scientists suggest that the L-arginine/ADMA ratio is a better index of NOS substrate availability and, thus, functional integrity of the NOS pathway, than L-arginine levels alone.

Publications

Citations


DuPont, JJ;Ramick, MG;Farquhar, WB;Townsend, RR;Edwards, DG;, NADPH oxidase-derived reactive oxygen species contribute to impaired cutaneous microvascular function in chronic kidney disease, Am. J. Physiol. Renal Physiol., 2014, Issue 12, Vol. 306, Pg. F1499-506, https://ajprenal.physiology.org/content/ajprenal/early/2014/04/21/ajprenal.00058.2014.full.pdf

Li, H;Zhou, Y;Zhao, A;Qiu, Y;Xie, G;Jiang, Q;Zheng, X;Zhong, W;Sun, X;Zhou, Z;Jia, W;, Asymmetric dimethylarginine attenuates serum starvation-induced apoptosis via suppression of the Fas (APO-1/CD95)/JNK (SAPK) pathway, Cell Death Dis, V4, pg e830, 2013https://www.nature.com/cddis/journal/v4/n10/full/cddis2013345a.html

Schulze F, Wesemann R, Schwedhelm E, Sydow K, Albsmeier J, Cooke JP, Bager RH. Determination of ADMA using a novel ELISA assay. Clin. Chem. Lab. Med. 2004; 42: 1377-1383

Manual

Product Manual