Analytical Data
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Gene name
ST6GAL1
- Application
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Alternative Names
B-cell antigen CD75 CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1 ST6Gal I
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P15907
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Expression Region
1-406aa
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Molecular Weight
52.1 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
ST6GAL1, also known as ST6 beta-galactosamide alpha-2,6-sialyltransferase 1, is an important enzyme involved in the biosynthesis of sialylated glycan structures on glycoproteins and glycolipids. Sialic acids are key components that modulate cellular interactions, immune responses, and the stability of glycoproteins. Dysregulation of ST6GAL1 has been implicated in various biological processes, including cancer progression, as it influences tumor cell behavior and the immune evasion mechanisms of cancer cells. Additionally, ST6GAL1 plays a crucial role in neuronal development and function, making its study relevant in neuroscientific research. Recent advancements in recombinant protein technology have enabled the production of ST6GAL1 in heterologous systems, allowing for a better understanding of its function and mechanisms. By studying the recombinant form of ST6GAL1, researchers aim to elucidate its specific role in sialic acid transfer, the resulting effects on glycan structures, and its implications in health and disease. This research holds significance not only for basic science but also for potential therapeutic interventions targeting ST6GAL1 in diseases associated with altered sialylation patterns.
