Anti-AMD1 Antibody Picoband® Fluoro647 Conjugated

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.

Cancer, Cell Biology, Energy Metabolism, Energy Transfer Pathways, Metabolic Signaling Pathways, Metabolism, Pathways and Processes, Signal Transduction

Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels.

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