Polyclonal Anti-SAMDC

Rabbit IgG polyclonal antibody for S-adenosylmethionine decarboxylase proenzyme (AMD1) detection. Tested with WB, IHC-P in Human;Mouse;Rat. \n

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SPECIFICATIONS

Price

200.00 USD

Catalog Number

PA1070

Size

100ug/vial

Applications

IHC, WB

Reactivities

Hum, Mouse, Rat

Form

Lyophilized

Format

Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.

Gene Id

AMD1

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.

Swiss Prot

P17707

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.\nAvoid repeated freezing and thawing. \n\"\n

Additional Info

A synthetic peptide corresponding to a sequence at the C-terminal of human SAMDC, identical to the related mouse and rat sequences.

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.