Analytical Data
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Gene name
ST3GAL3
- Application
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Alternative Names
Beta-galactoside alpha-2,3-sialyltransferase 3 ;Alpha 2,3-ST 3Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferaseN-acetyllactosaminide alpha-2,3-sialyltransferase;ST3Gal III ;ST3GalIIIST3NSialyltransferase 6
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q11203
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Expression Region
29-375aa
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Molecular Weight
54.9 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
ST3GAL3, a member of the sialyltransferase family, is responsible for the transfer of sialic acid to glycoproteins and glycolipids, playing a crucial role in various biological processes, including cell adhesion, migration, and immune response. Dysregulation of ST3GAL3 has been implicated in several diseases, notably cancer, where it may influence tumor progression and metastasis by modifying the glycan structures on cell surfaces. In addition, altered ST3GAL3 activity has been associated with inflammatory responses and neurological disorders. Given its significant biological functions, the recombinant study of ST3GAL3 protein is pivotal for understanding its mechanistic roles in disease etiology and progression. Researchers aim to produce ST3GAL3 as a recombinant protein to facilitate structural and functional analyses, paving the way for potential therapeutic applications. Insights gained from these studies could lead to the development of targeted therapies that manipulate sialylation pathways, thereby offering new avenues for intervention in diseases where ST3GAL3 is implicated. The ongoing research on ST3GAL3 recombinant protein not only enhances our understanding of glycan dynamics but also holds promise for innovative strategies in biomedical research and clinical practices.
