Analytical Data
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Gene name
NAGS
- Application
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Alternative Names
NAGS；N-acetylglutamate synthase. mitochondrial
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8N159
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Expression Region
1-534aa
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AA Sequence
MATALMAVVLRAAAVAPRLRGRGGTGGARRLSCGARRRAARGTSPGRRLSTAWSQPQPPPEEYAGADDVSQSPVAEEPSWVPSPRPPVPHESPEPPSGRSLVQRDIQAFLNQCGASPGEARHWLTQFQTCHHSADKPFAVIEVDEEVLKCQQGVSSLAFALAFLQRMDMKPLVVLGLPAPTAPSGCLSFWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASYGGIVSVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPHHSSAVITAASTLLTELFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLASLRPRLHSIYVSEGYNAAAILTMEPVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDSYELVNHAKGLPDSFHKPASDPGS
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Molecular Weight
58.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
NAGS (N-acetylglutamate synthetase) is a crucial enzyme involved in the metabolism of amino acids, specifically playing a key role in the urea cycle by facilitating the synthesis of N-acetylglutamate, which is an essential activator of carbamoyl phosphate synthetase I. Disorders related to NAGS can lead to hyperammonemia, a potentially life-threatening condition. The study of NAGS recombinant protein is paramount for understanding its structure-function relationship and the underlying biological mechanisms. Advances in recombinant DNA technology enable the production of NAGS in host systems, providing a valuable tool for examining its enzymatic activity and regulatory mechanisms. Furthermore, characterizing NAGS through recombinant approaches can aid in the development of therapeutic strategies for treating metabolic disorders associated with its deficiency. Research efforts are focused on elucidating the enzyme's kinetics, stability, and interaction with other metabolic pathways, contributing to a deeper understanding of its role in amino acid metabolism and potential implications for gene therapy. Overall, the exploration of NAGS recombinant protein presents significant opportunities for both basic biochemistry and clinical applications in metabolic disease management.
