Analytical Data
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Gene name
NAGK
- Application
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Alternative Names
GlcNAc kinase
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UJ70
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Expression Region
2-344aa
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Molecular Weight
53.2 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
N-acetylglucosamine kinase (NAGK) plays a critical role in the hexosamine biosynthetic pathway, which is essential for the post-translational modifications of proteins and the synthesis of glycoproteins and glycolipids. The enzyme catalyzes the phosphorylation of N-acetylglucosamine (GlcNAc) to N-acetylglucosamine-6-phosphate, a key intermediate for numerous cellular processes, including the regulation of gene expression and the maintenance of cellular homeostasis. Dysregulation of this pathway has been associated with metabolic disorders, such as diabetes and obesity, and has implications in cancer progression and neurodegenerative diseases. Consequently, understanding the structure and function of NAGK has garnered significant interest in various fields of biomedical research. Recent studies employ recombinant protein techniques to produce and purify NAGK, allowing for detailed kinetic and structural analyses. These investigations aim to elucidate the enzyme's catalytic mechanism and regulatory properties, providing insights that could lead to the development of specific inhibitors or modulators. As researchers continue to explore the potential therapeutic applications of targeting NAGK, the recombinant expression of this enzyme serves as a vital tool for drug discovery and the development of novel treatments for related diseases.
