Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
The N-acetylglutamate synthase gene encodes a mitochondrial enzyme that catalyzes the formation of N-acetylglutamate (NAG) from glutamate and acetyl coenzyme-A. Additionally we are shipping NAGS Proteins (25) and NAGS Kits (2) and many more products for this protein.
Showing 10 out of 16 products:
The specificity of the assay was validated by demonstrating a complete deficiency of NAGS in liver homogenates from Nags -/- mice. CONCLUSION: The novel NAGS enzyme assay reported herein can be used for the diagnosis of inherited NAGS deficiency and may also be of value in the study of secondary hyperammonemia present in various inborn errors of metabolism as well as drug treatment.
Results identified 36 NAGS mutations in NAGSD patients; 61% of which are missense mutations. Phenotypes associated with these mutations in the GNAT domain are more severe than phenotypes of that of amino acid kinase domain. Enzyme activity and stability assays with 12 mutations, together with in silico structural analysis, support the pathogenic role of most NAGSD-associated mutations found.
Data indicate the formation of alternative N-acylglutamates by N-acetylglutamate synthase (NAGS).
Sp1 (show PSG1 Antibodies), CREB (show CREB1 Antibodies), HNF-1 (show HNF1A Antibodies), and NF-Y, known to be responsive to hormones and diet, regulate NAGS transcription
NAGS deficiency in humans leads to hyperammonemia and can be primary, due to mutations in the NAGS gene or secondary due to other mitochondrial aberrations that interfere with the normal function of the same enzyme.
After the human NAGS gene was identified, mutation analysis revealed that the older sibling on NCG therapy was homozygous for a 971G>A (W324X) mutation.
The first mutation in NAGS has been reported in a family with carbamylglutamate responsive hyperammonemia and normal activity of the urea cycle enzymes.
Gene product expressed in E. coli shown to have NAGS enzyme activity. Gene name provisionally was assigned as NAT7.
report two deleterious mutations within the NAGS gene found in two families with infants presenting with acute neonatal disease; finding confirms the genetic origin of NAGS deficiency
first report of mutation analysis in a series of families affected with deficiency of NAGS
The intestinal NAGS mRNA levels were lower in 7- to 28-day-old than in 1-day-old pigs. Immunochemical analysis revealed that NAGS protein was localized in enterocytes of the gut (show GUSB Antibodies).
Sp1 (show SP1 Antibodies), CREB (show CREB1 Antibodies), HNF-1 (show HNF1A Antibodies), and NF-Y, known to be responsive to hormones and diet, regulate NAGS transcription
Is a mitochondrial enzyme that catalyzes the formation of N-acetylglutamate (NAG (show SCN7A Antibodies))
The biochemical properties of purified recombinant human and mouse NAGS-M and NAGS-C were determined in this study with the goal of better understanding the role of the variable domain in NAGS function.
The N-acetylglutamate synthase gene encodes a mitochondrial enzyme that catalyzes the formation of N-acetylglutamate (NAG) from glutamate and acetyl coenzyme-A. NAG is a cofactor of carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle in mammals. This gene may regulate ureagenesis by altering NAG availability and, thereby, CPSI activity. Deficiencies in N-acetylglutamate synthase have been associated with hyperammonemia.
, N-acetylglutamate synthase, mitochondrial
, amino-acid acetyltransferase
, amino-acid N-acetyltransferase