Analytical Data
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Gene name
GNPNAT1
- Application
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Alternative Names
GNPNAT1;GNA1;Glucosamine 6-phosphate N-acetyltransferase
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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
Q96EK6
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Expression Region
1-184aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMKPDETPMFDPSLLKEVDWSQNTATFS PAISPTHPGEGLVLRPLCTADLNRGFFKVLGQLTETGVVSPEQFMKSFEH MKKSGDYYVTVVEDVTLGQIVATATLIIEHKFIHSCAKRGRVEDVVVSDE CRGKQLGKLLLSTLTLLSKKLNCYKITLECLPQNVGFYKKFGYTVSEENY MCRRFLK
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Molecular Weight
23 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
GNPNAT1 (GlcNAc-1-phosphate transferase 1) is an enzyme that plays a critical role in glycosylation, specifically in the modification of proteins and lipids through the addition of N-acetylglucosamine (GlcNAc) moieties. This process is essential for various cellular functions, including protein stability, signaling, and cellular interactions. Recent studies have highlighted the importance of GNPNAT1 in the context of several diseases, particularly in neurodegenerative disorders and certain cancers, where aberrant glycosylation patterns are observed. Understanding the structure and function of GNPNAT1 is crucial for deciphering its biological significance and potential as a therapeutic target. Recombinant GNPNAT1 proteins have been produced to facilitate detailed biochemical studies, including enzyme kinetics, substrate specificity, and interactions with other glycosylation-related enzymes. These studies aim to elucidate the mechanistic pathways involving GNPNAT1 and its contribution to cellular homeostasis. Furthermore, the generation of antibodies against GNPNAT1 has enabled its localization and role in various biological contexts to be explored. The ongoing research into GNPNAT1 not only broadens our understanding of glycosylation but also opens avenues for developing novel diagnostic and therapeutic strategies for diseases associated with glycosylation abnormalities.
