recommended for detection of Atase of human origin by WB, IP and ELISA
Modification Notes
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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPELISA
WB:1:500~1:2000 IP:1:100~1:500 Notes:Optimal dilutions/concentrations should be determined by the researcher.
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
recommended for detection of Atase of human origin by WB IP and ELISA
Tissue Specificity
recommended for detection of Atase of human origin by WB, IP and ELISA