Analytical Data
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Gene name
ST3GAL6
- Application
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Alternative Names
Type 2 lactosamine alpha-2.3-sialyltransferase. EC:2.4.3.6. CMP-NeuAc:beta-galactoside alpha-2.3-sialyltransferase VI. ST3Gal VI. ST3GalVI. Sialyltransferase 10
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y274
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Expression Region
145-240 aa
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AA Sequence
MNNGPVLGHEEEVGRRTTFRLFYPESVFSDPIHNDPNTTVILTAFKPHDLRWLLELLMGDKINTNGFWKKPALNLIYKPYQIRILDPFIIRTAAYE
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Molecular Weight
36.3 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
ST3GAL6, a member of the sialyltransferase family, plays a crucial role in the post-translational modification of glycoproteins and glycolipids through the addition of sialic acid residues. These modifications are essential for various biological processes, including cell-cell interactions, immune response, and tumor progression. Research has shown that altered expression of ST3GAL6 is linked to several pathological conditions, including cancers and inflammatory diseases, suggesting its potential as a therapeutic target or biomarker. The reconstitution and expression of ST3GAL6 as a recombinant protein enable detailed studies of its enzymatic activity, substrate specificity, and regulatory mechanisms. Understanding its structure-function relationship could provide insights into its role in glycosylation pathways and offer opportunities for developing novel strategies to modulate sialylation, which may have therapeutic implications in diseases characterized by aberrant glycosylation patterns. This research area is significant in enhancing our understanding of cell biology and disease mechanisms, paving the way for innovative treatment approaches.
