Analytical Data
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Gene name
MGAT1
- Application
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Alternative Names
(N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I)(GNT-I)(GlcNAc-T I)
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Species
Rabbit
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P27115
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Expression Region
30-447aa
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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
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Protein Description
MGAT1 (Mannosyl-oligosaccharide Glucosidase I) is a crucial enzyme involved in the glycosylation process of proteins, contributing significantly to the proper folding and functionality of glycoproteins in both prokaryotic and eukaryotic organisms. Understanding its structure and function is essential for various applications, including biotechnology and pharmaceuticals. The research on recombinant MGAT1 proteins has gained momentum due to their potential in enhancing the production of therapeutic glycoproteins and in the study of glycosylation-related diseases. Producing MGAT1 as a recombinant protein allows for detailed biochemical characterization, including its enzymatic activity, substrate specificity, and interactions with other glycosylation enzymes. Additionally, studying MGAT1 can provide insights into the pathway of glycan biosynthesis, which is vital for the development of strategies to manipulate glycosylation patterns for therapeutic purposes. Recent advancements in genetic engineering and expression systems have made it feasible to produce high yields of functional MGAT1, paving the way for further research into its application in glycoprotein production, drug development, and understanding glycosylation disorders. As researchers continue to delve deeper into the role of MGAT1, the implications of their findings could lead to significant breakthroughs in regenerative medicine and targeted therapeutics.
