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.

Optimal dilution of the AMD1 antibody should be determined by the researcher.

Amino acids RKNFMKPSHQGYPHRNFQEEIEFLNA were used as the immunogen for the AMD1 antibody.

After reconstitution, the AMD1 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.