Background:

AdoMetDC (adenosylmethionine decarboxylase 1), also known as S-adenosylmethionine decarboxylase proenzyme (SAMDC) or AMD1, is a 334 amino acid protein which is an important intermediate enzyme in polyamine biosynthesis pathways. Using a pyruvoyl group as a cofactor, AdoMetDC catalyzes the conversion of S-adenosyl-L-methionine to (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt and carbon dioxide. AdoMetDC is synthesized as an inactive proenzyme that undergoes self-maturation to form two non-identical subunits designated α and β. Active AdoMetDC forms a heterotetramer of two α chains and two β chains. Both AdoMetDC proenzyme processing and mature AdoMetDC catalytic activity are stimulated by putrescine, while catalytic activity is inhibited by iodoacetic acid.

Specificity:

AMD1 polyclonal antibody detects endogenous levels of AMD1 protein.

Alternative names:

S-adenosylmethionine decarboxylase proenzyme; AdoMetDC; SAMDC; S-adenosylmethionine decarboxylase alpha chain; S-adenosylmethionine decarboxylase beta chain; AMD

Species reactivity:

Human,Mouse

Host:

Rabbit

Ig type:

Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2

Immunogen:

A synthetic peptide corresponding to residues in Human AMD1.

Purification & Purity:

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

Molecular weight:

~ 38 kDa

Applications:

WB

Usage:

WB: 1:500~1:1000

Storage:

Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.

Precautions:

For research use only, not for use in diagnostic procedure.

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