Analytical Data
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Gene name
GNTI
- Application
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Alternative Names
(N-acetylglucosaminyltransferase I)(GlcNAcT-I)(N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I)(Protein COMPLEX GLYCAN LESS 1)
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Species
Arabidopsis thaliana
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Source
Baculovirus
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9XGM8
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Expression Region
25-444aa
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Molecular Weight
51.6 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
GNTI, or GlcNAc-1-phosphate uridyltransferase, is an enzyme that plays a pivotal role in the biosynthesis of glycoproteins and glycolipids, which are essential for numerous biological processes including cell signaling, immune response, and cellular communication. The research on recombinant GNTI has gained significant attention due to its potential applications in biotechnology and medicine. By producing GNTI as a recombinant protein, scientists aim to better understand its structure-function relationships, catalytic mechanisms, and the pathways it participates in. This research is critical for developing therapeutic strategies for diseases linked to glycosylation defects, which can lead to various disorders, including congenital disorders of glycosylation. Additionally, understanding GNTI could facilitate the engineering of glycoproteins with improved efficacy and stability for use in drug development. The ability to produce GNTI in a controlled manner allows for high-throughput screening of its activity and interactions, ultimately contributing to advancements in glycobiology and the development of novel glycan-based therapeutics.
