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Polyclonal Anti-SAMDC

Cat no: PA1070


Supplier: Boster Immunoleader
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Rabbit IgG polyclonal antibody for S-adenosylmethionine decarboxylase proenzyme (AMD1) detection. Tested with WB, IHC-P in Human;Mouse;Rat.
Catalogue number: PA1070
Price: $200.00
Reactivities: Human, Mouse, Rat
Applications: Immunohistochemistry, Western Blot
Size: 100ug/vial
Gene: AMD1
Swiss prot: P17707
Form: Lyophilized
Format: Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.
Storage temp: "At -20 degree C for one year. After reconstitution, at 4 degree C for one month. It can also be aliquotted and stored frozen at -20 degree C for a longer time. Avoid repeated freezing and thawing. "
Scientific background: 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.
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. 2. 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. 3. 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. 4. 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: A synthetic peptide corresponding to a sequence at the C-terminal of human SAMDC, identical to the related mouse and rat sequences.