Atase (amidophosphoribosyltransferase), also known as PPAT (phosphoribosyl pyrophosphate (PRPP) amidotransferase), PRAT or GPAT (glutamine phosphoribosyl pyrophosphate amidotransferase), is a ubiquitously expressed N-terminal nucleophile-type glutamine amidotransferase that belongs to the purine/pyrimidine phosphoribosyltransferase family. Existing as a homotetramer, Atase plays an important role in purine metabolism. More specifically, Atase functions as regulatory enzyme and contains one glutamine amidotransferase type-2 domain. Binding a magnesium ion and a 4Fe-4S cluster as cofactors, Atase catalyzes the first step (the rate-limiting step) in the purine nucleotide biosynthesis pathway, a two-step reaction that results in the formation of phosphoribosylamine from PRPP and glutamine. The first step of this reaction is catalyzed by the N-terminal glutaminase domain while the second step is catalyzed by the C-terminal PRTase domain.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB 1:500 - 1:2000
Application Notes:
PPAT polyclonal antibody detects endogenous levels of PPAT protein.
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