AMD1 pAb

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 (alpha) and ?. Active AdoMetDC forms a heterotetramer of two (alpha) chains and two ? chains. Both AdoMetDC proenzyme processing and mature AdoMetDC catalytic activity are stimulated by putrescine, while catalytic activity is inhibited by iodoacetic acid.

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SPECIFICATIONS

Catalog Number

BS60408

Size

100ug/100ul

Applications

WB

Hosts

Rabbit

Reactivities

Hum, Mouse, Rat

Form

liquid

Purity

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

Antigen

A synthetic peptide corresponding to residues in Human AMD1.

Species

AMD1 pAb detects endogenous levels of AMD1 protein.

Dilutions

WB: 1:500~1:1000\r

Swiss Prot

P17707

Storage Temp

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

Concentration

1ug/ul

Storage Buffer

1 mg/ml in Phosphate buffered saline (PBS) with 0.05% sodium azide, approx. pH 7.2.

Additional Info

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

Molecular Weight

~ 38 kDa

Alternative Names

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