Analytical Data
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Gene name
Mgat3
- Application
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Alternative Names
(N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III)(GNT-III)(GlcNAc-T III)(N-acetylglucosaminyltransferase III)
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Species
Mouse
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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
Q10470
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Expression Region
24-538aa
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Molecular Weight
66.6 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
Mgat3, or mannose-β-1,4-N-acetylglucosaminyltransferase 3, is a critical enzyme involved in the biosynthesis of N-glycans, which are essential glycoprotein structures that influence various biological processes, including cell signaling, immune response, and protein stability. The enzyme catalyzes the transfer of N-acetylglucosamine (GlcNAc) to mannose residues on glycoproteins, thus playing a significant role in the formation of complex N-glycan structures. Research into Mgat3 has gained importance due to its implications in diverse fields such as cancer biology, where altered N-glycosylation patterns are linked to tumor progression and metastasis. Furthermore, Mgat3 activity is associated with the modulation of the immune response; for instance, its expression can affect the binding affinity of glycoproteins to specific receptors, influencing cellular interactions. Understanding the structure and function of Mgat3, along with its regulatory mechanisms, can provide insights into therapeutic strategies for diseases characterized by aberrant glycosylation. In recent years, recombinant protein production of Mgat3 has become a valuable tool for studying its enzymatic properties and interactions, facilitating the development of potential inhibitors or modulators as therapeutic agents. Consequently, the study of Mgat3 not only enhances our knowledge of glycosylation biology but also paves the way for innovative approaches in treating glycan-related diseases.
