Analytical Data
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Gene name
ST6GALNAC4
- Application
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Alternative Names
3-Gal-beta-1; 3-GalNAc-alpha-2; 6-sialyltransferase; Alpha-N-acetyl-neuraminyl-2.3-beta-galactosyl-1.3-N-acetyl-galactosaminide alpha-2.6-sialyltransferase; NeuAc-alpha-2; SIA7D_HUMAN; Sialyltransferase 3C; Sialyltransferase 7D; SIAT3-C; SIAT3C; SIAT7-D; SIAT7D; ST6GalNAc IV; St6galnac4; ST6GalNAcIV
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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
Q9H4F1
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Expression Region
1-302 aa
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AA Sequence
MKAPGRLVLIILCSVVFSAVYILLCCWAGLPLCLATCLDHHFPTGSRPTVPGPLHFSGYSSVPDGKPLVREPCRSCAVVSSSGQMLGSGLGAEIDSAECVFRMNQAPTVGFEADVGQRSTLRVVSHTSVPLLLRNYSHYFQKARDTLYMVWGQGRHMDRVLGGRTYRTLLQLTRMYPGLQVYTFTERMMAYCDQIFQDETGKNRRQSGSFLSTGWFTMILALELCEEIVVYGMVSDSYCREKSHPSVPYHYFEKGRLDECQMYLAHEQAPRSAHRFITEKAVFSRWAKKRPIVFAHPSWRTE
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Molecular Weight
60.6 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
ST6GALNAC4, a member of the sialyltransferase family, plays a critical role in the post-translational modification of glycoproteins and glycolipids by adding sialic acid residues to terminal galactose and N-acetylgalactosamine moieties. This enzymatic activity is essential for modulating various biological processes, including cell-cell interactions, immune response, and pathogen recognition, thus influencing cellular behaviors and disease susceptibility. Research on ST6GALNAC4 has gained momentum due to its implications in several pathological conditions, including cancer metastasis and neurodegenerative diseases. For instance, altered expression of ST6GALNAC4 has been linked to the aggressive phenotypes of certain tumor types, where changes in glycosylation patterns can facilitate tumor progression and immune evasion. Understanding the molecular mechanisms and functional consequences of ST6GALNAC4 activity may provide insights into targeted therapeutic strategies for diseases associated with aberrant glycosylation. Recently, the production of recombinant ST6GALNAC4 proteins allows for detailed structural and functional studies, enabling researchers to elucidate the enzyme's specificity, kinetics, and the impact of genetic variations. These recombinant proteins serve as valuable tools for assessing the role of sialylation in cell signaling pathways and developing potential pharmacological agents that could modulate sialyltransferase activities for therapeutic benefit. As such, the exploration of ST6GALNAC4 through recombinant technologies represents a promising avenue for advancing our understanding of sialylation in health and disease.
