S-adenosylmethionine decarboxylase proenzyme (AdoMetDC, SAMDC)

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.\n\nUniProt Number:\nP17707\n\nGene ID:\nAMD1\n\nApplications:\nSuitable for use in Western Blot and Immunohistochemistry (Paraffin).\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Handling:\nStore at -20?C for one year. After reconstitution, store at 4?C for one month. Can also be aliquoted and stored frozen at -20?C for long term.\nAvoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

145140

Size

100ug

Applications

IHC, WB

Hosts

Rabbit

Reactivities

Hum, Mouse, Rat

Form

Supplied as a lyophilized powder. Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. Reconstitution: Add 0.2ml of distilled water will yield a concentration of 500ug/ml.

P Type

Pab

Purity

Purified by immunoaffinity chromatography.

Isotype

IgG

References

1. Maric SC, Crozat A, Louhimo J, Knuutila S, Janne OA. The human S-adenosylmethionine decarboxylase gene: nucleotide sequence of a pseudogene and chromosomal localization of the active gene (AMD1) and the pseudogene (AMD2). Cytogenet Cell Genet. 1995; 70(3-4):195-9. \n2. Hill JR, Morris DR. Cell-specific translation of S-adenosylmethionine decarboxylase mRNA. Regulation by the 5' transcript leader. J Biol Chem. 1992 Oct 25; 267(30):21886-93.\n3. Ekstrom JL, Mathews II, Stanley BA, Pegg AE, Ealick SE The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold. Structure. 1999 May; 7(5):583-95. \n4. Morrison LD, Becker L, Kish SJ. S-adenosylmethionine decarboxylase in human brain. Regional distribution and influence of aging. Brain Res Dev Brain Res. 1993 Jun 8; 73(2):237-41.

Additional Info

Recognizes human, mouse and rat SAMDC. No crossreactivity with other proteins.