Anti-AMD1 / S-adenosylmethionine decarboxylase

0.5mg/ml if reconstituted with 0.2ml sterile DI water. S-adenosylmethionine decarboxylase (AdoMet-DC), also known as S-adenosylmethionine decarboxylase proenzyme (SAMDC) or AMD1, is a key enzyme in polyamine biosynthesis. It is localized to chromosome region 6q21-q22. SAMDC has an unusual distribution in polysomes from cells of T lymphocyte origin. It associates predominantly with monosomes and small polysomes with none located in the preribosomal or ribonucleoprotein pool. SAMDC is a critical regulatory enzyme of the polyamine synthetic pathway, and a well-studied drug target. Since SAMDC is a key regulatory enzyme in the synthesis of spermidine and spermine, the marked increase in SAMDC activity in the neonate and the sustained high enzyme levels throughout adulthood, imply a role for these polyamines in both development and mature brain function. Protein function: Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels. [The UniProt Consortium]