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NSJ Bioreagents

SKU:R32969

AMD1 Antibody / S-adenosylmethionine decarboxylase

AMD1 Antibody / S-adenosylmethionine decarboxylase

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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.

Specifications

Family Primary antibody
Formulation 0.5mg/ml if reconstituted with 0.2ml sterile DI water
Format Antigen affinity purified
Host Animal Rabbit
Clonality Polyclonal (rabbit origin)
Isotype Rabbit IgG
Species Reactivity Human, Mouse, Rat
Application WB, IHC-P
Application Details Western Blot: 0.5-1ug/ml,IHC (FFPE): 1-2ug/ml
Application Note Optimal dilution of the AMD1 antibody should be determined by the researcher.
Localization Cytoplasmic
Immunogen Amino acids RKNFMKPSHQGYPHRNFQEEIEFLNA were used as the immunogen for the AMD1 antibody.
Buffer Lyophilized from 1X PBS with 2.5% BSA, 0.025% sodium azide
Purity Antigen affinity
Storage 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.
Limitation This AMD1 antibody is available for research use only.
Uniprot # P17707
Status Available
PDF Link https://www.nsjbio.com/tds-pdf/amd1-antibody-s-adenosylmethionine-decarboxylase-r32969
Title AMD1 Antibody / S-adenosylmethionine decarboxylase
Description 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.
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