Application

SAH is suitable for use:

to investigate whether AdoHcy competes with AdoMet in the down-regulation of reporter activity of LUC reporter gene
as a reagent to study the abundance patterns of SAH and its correlation with vertebrate metamorphosis
in the optimization of the protein (lysine K) methyltransferase SET7/9 activity assay
in the fluorescence polarization (FP) assay during dengue virus methyltransferase activity measurement
as a standard for the measurement of SAH from blood samples by high performance liquid chromatography (HPLC) with fluorimetric detection method

Biochem/physiol Actions

S-(5′-Adenosyl)-L-homocysteine (AdoHcy/SAH) is a component of intracellular homocysteine stress. AdoHcy is a competitive inhibitor (versus AdoMet) of DNA methyltransferases (S-adenosyl-L-methionine (AdoMet)-dependent methyltransferases) involved in epigenetics. Consequently, AdoHcy is used in a variety of studies on epigenetics in hyperhomocysteinemic states. AdoHcy is metabolized by S-adenosylhomocysteine hydrolase (AHCY). AdoHcy is the product of enzymatic transmethylation reactions involving S-Adenosylmethionine (SAM). It is reconverted to SAM by its cleavage into adenosine and L-homocysteine, a substrate of thetin-homocysteine S-methyltransferase. The concentration alterations of SAM and SAH in plasma serve as predictors of cellular methylation potential and metabolic alterations. Methylation capacity indicates specific genetic polymorphisms and/or nutritional deficiencies. Methylation is important in epigenetics, reprogramming, and cancer.