Technical Data
AMD1 (SAMDC , S-adenosylmethionine Decarboxylase Proenzyme, AdoMetDC, S-adenosylmethionine Decarboxylase alpha Chain, S-adenosylmethionine Decarboxylase beta Chain, AMD1, AMD)
S-adenosylmethionine decarboxylase (AdoMet-DC), also known as S-adenosylmethionine decarboxylase proenzyme (SAMDC), 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.

Suitable for use in Western Blot. Other applications not tested.

Recommended Dilution:
Optimal dilutions to be determined by the researcher.

AA Sequence:

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
PabIgGAffinity Purified
50ug-20CBlue IceHumanMouse
As reported
Full length human AMD1, aa1-334 (NP_001625.2)
Purified by Protein A affinity chromatography.
Supplied as a liquid in PBS, pH 7.2.
Recognizes human AMD1.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.