Analytical Data
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Gene name
D-Gal
- Application
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Alternative Names
D-Gal；SIAT3C；SIAT7D；Alpha-N-acetyl-neuraminyl-2.3-beta-galactosyl-1.3-N-acetyl-galactosaminide alpha-2.6-sialyltransferase
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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
Q9H4F1
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Expression Region
1-302aa
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AA Sequence
MKAPGRLVLIILCSVVFSAVYILLCCWAGLPLCLATCLDHHFPTGSRPTVPGPLHFSGYSSVPDGKPLVREPCRSCAVVSSSGQMLGSGLGAEIDSAECVFRMNQAPTVGFEADVGQRSTLRVVSHTSVPLLLRNYSHYFQKARDTLYMVWGQGRHMDRVLGGRTYRTLLQLTRMYPGLQVYTFTERMMAYCDQIFQDETGKNRRQSGSFLSTGWFTMILALELCEEIVVYGMVSDSYCREKSHPSVPYHYFEKGRLDECQMYLAHEQAPRSAHRFITEKAVFSRWAKKRPIVFAHPSWRTE
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Molecular Weight
34.2 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
D-Galactose (D-Gal) is a monosaccharide that plays a significant role in various biological processes, including cellular signaling, energy metabolism, and the structural composition of glycoproteins and glycolipids. The study of D-Gal recombinants, particularly in the context of protein engineering, has gained traction due to its potential applications in biotechnology and therapeutics. Researchers have been focusing on the enzymatic pathways involving D-Gal, such as the metabolism of galactose in organisms, exploring how specific enzymes or proteins can be modified to enhance activity or specificity. Additionally, the implications of D-Gal in human health, such as its involvement in age-related diseases and metabolic disorders, have prompted investigations into recombinant proteins that utilize D-Gal for drug delivery systems or as therapeutic agents. The development of recombinant proteins that interact with D-Gal can lead to innovative approaches in treating conditions associated with glycosylation disorders, thereby expanding our understanding of carbohydrate metabolism and its impact on health. Through genetic engineering techniques, D-Gal recombinants are being used to create proteins with novel functionalities, contributing to advancements in enzyme replacement therapies and the design of biocatalysts for industrial applications. Overall, the research on D-Gal recombinant proteins holds promise for both enhancing our understanding of metabolic pathways and developing new biotechnological solutions.
