-
-
Overview
-
AMD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 292 amino acids (68-334) and having a molecular mass of 33.4 kDa. AMD1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. Adenosylmethionine decarboxylase proenzyme (AMD1) is synthesized originally as an inactive proenzyme. Putrescine stimulates both the proenzyme processing and the catalytic activity. The catalytic activity is inhibited by iodoacetic acid. The active enzyme formation entails a self-maturation process in which the active site pyruvoyl group is produced from an internal serine residue using an autocatalytic post-translational modification.
Please contact us at for specific academic pricing.
-
- Properties
-
Overview