金山科研平台，产品价格货期咨询微信：jinshanbio Source:E. coli-derived, Ser2-Tyr432, with an N-terminal Met and 6-His tag Accession #:P23526 N-terminal Sequence Analysis:Met Purity:>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 µg per lane. Endotoxin Level: Predicted Molecular Mass:49 kDa SDS-PAGE:43 kDa, reducing conditions Activity:Measured by the hydrolysis of S-adenosyl-L-homocysteine.The specific activity is >350 pmol/min/µg, as measured under the described conditions. Formulation:Supplied as a 0.2 µm filtered solution in Tris, NaCl and Glycerol.See Certificate of Analysis for details. Molecule Information: Adenosylhomocysteinase/AHCY Aliases: AdoHcyase; AHCY; SAHH Entrez Gene IDs: 191 (Human) Background: Adenosylhomocysteinase Human S-Adenosylhomocysteinase (AHCY) is a cytoplasmic tetramer with a tightly bound NAD co-factor for each subunit. It is the only known enzyme to catalyze the breakdown of S-adenosylhomocysteine (AdoHcy) to homocysteine and adenosine. AdoHcy hydrolysis is a reversible reaction with an equilibrium favoring AdoHcy formation, but hydrolysis prevails under physiological conditions due to the rapid removal of adenosine and homocysteine. Thus, AHCY's activity in mammals is directly related to homocysteine level, an independent risk factor for vascular disease. It also functions as a regulator of biological transmethylation by controlling the concentration of AdoHcy, a potent competitive inhibitor of all S-adonosyl-L-methionine methyltransferases. A mutation in the human AHCY results in AHCY deficiency with increase of plasma creatine kinase, methionine, S-adenosylmethionine and AdoHcy, delay of myelination, myopathy and psychomotor retardation.