Phosphoribosyl Pyrophosphate Amidotransferase Antibody [M15J4] Datasheet

Biological Description

Specificity	Phosphoribosyl Pyrophosphate Amidotransferase Antibody [M15J4] detects endogenous levels of total Phosphoribosyl Pyrophosphate Amidotransferase protein.
Background	Phosphoribosyl pyrophosphate amidotransferase (PPAT, amidophosphoribosyltransferase) is the first committed enzyme of the de novo purine biosynthetic pathway and belongs to the purine/pyrimidine phosphoribosyltransferase family that channels carbon and nitrogen from basic metabolites into nascent AMP and GMP pools. The polypeptide contains an N‑terminal glutaminase domain and a C‑terminal phosphoribosyltransferase domain, and these two modules cooperate so that glutamine is hydrolyzed to release ammonia, which then travels through an internal channel to the transferase site where it attacks 5‑phosphoribosyl‑1‑pyrophosphate (PRPP) and generates 5‑phosphoribosylamine as the first nitrogen‑containing intermediate of the pathway. This internal channeling of ammonia prevents diffusion and unwanted hydrolysis of labile intermediates and couples glutamine turnover tightly to productive formation of 5‑phosphoribosylamine, allowing PPAT to act as an efficient gatekeeper that sets the overall flux into purine synthesis. Each subunit carries allosteric binding pockets that accommodate end products such as AMP, GMP, ADP, and GDP, and binding of specific nucleotide pairs at overlapping catalytic and allosteric sites stabilizes conformations in which the flexible glutamine loop is held open, limiting PRPP binding and shutting down catalysis. Through this feedback inhibition, PPAT integrates information on cellular adenine and guanine nucleotide pools and adjusts the rate of new purine production so that supply matches demand during changes in proliferation, nutrient status, or stress. The enzyme sits early in a pathway that produces ATP and GTP for DNA and RNA synthesis, energy transfer, and signaling, so its activity has strong effects on cell‑cycle progression, DNA replication capacity, and survival in rapidly dividing cells. Elevated PPAT expression has been documented in several solid tumors, including thyroid carcinoma, where high enzyme levels associate with increased proliferation, altered metabolic rewiring, and poor prognosis, linking de novo purine synthesis control directly to oncogenic growth behavior.

Specificity

Phosphoribosyl Pyrophosphate Amidotransferase Antibody [M15J4] detects endogenous levels of total Phosphoribosyl Pyrophosphate Amidotransferase protein.

Background

Phosphoribosyl pyrophosphate amidotransferase (PPAT, amidophosphoribosyltransferase) is the first committed enzyme of the de novo purine biosynthetic pathway and belongs to the purine/pyrimidine phosphoribosyltransferase family that channels carbon and nitrogen from basic metabolites into nascent AMP and GMP pools. The polypeptide contains an N‑terminal glutaminase domain and a C‑terminal phosphoribosyltransferase domain, and these two modules cooperate so that glutamine is hydrolyzed to release ammonia, which then travels through an internal channel to the transferase site where it attacks 5‑phosphoribosyl‑1‑pyrophosphate (PRPP) and generates 5‑phosphoribosylamine as the first nitrogen‑containing intermediate of the pathway. This internal channeling of ammonia prevents diffusion and unwanted hydrolysis of labile intermediates and couples glutamine turnover tightly to productive formation of 5‑phosphoribosylamine, allowing PPAT to act as an efficient gatekeeper that sets the overall flux into purine synthesis. Each subunit carries allosteric binding pockets that accommodate end products such as AMP, GMP, ADP, and GDP, and binding of specific nucleotide pairs at overlapping catalytic and allosteric sites stabilizes conformations in which the flexible glutamine loop is held open, limiting PRPP binding and shutting down catalysis. Through this feedback inhibition, PPAT integrates information on cellular adenine and guanine nucleotide pools and adjusts the rate of new purine production so that supply matches demand during changes in proliferation, nutrient status, or stress. The enzyme sits early in a pathway that produces ATP and GTP for DNA and RNA synthesis, energy transfer, and signaling, so its activity has strong effects on cell‑cycle progression, DNA replication capacity, and survival in rapidly dividing cells. Elevated PPAT expression has been documented in several solid tumors, including thyroid carcinoma, where high enzyme levels associate with increased proliferation, altered metabolic rewiring, and poor prognosis, linking de novo purine synthesis control directly to oncogenic growth behavior.

Usage Information

Application

WB, IHC

Dilution

WB	IHC
1:500-2000	1:150

Reactivity

Human, Mouse, Rat, Canine, Monkey

Source

Mouse Monoclonal Antibody

MW

57.2 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

References

https://pubmed.ncbi.nlm.nih.gov/35027843/

Phosphoribosyl Pyrophosphate Amidotransferase Antibody [M15J4]

Biological Description

Usage Information

References

Application Data