Analytical Data
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Gene name
ST6GAL1
- Application
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Alternative Names
ST6GAL1;SIAT1;Beta-galactoside alpha-2.6-sialyltransferase 1
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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
P15907
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Expression Region
27-406aa
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AA Sequence
KEKKKGSYYDSFKLQTKEFQVLKSLGKLAMGSDSQSVSSSSTQDPHRGRQ TLGSLRGLAKAKPEASFQVWNKDSSSKNLIPRLQKIWKNYLSMNKYKVSY KGPGPGIKFSAEALRCHLRDHVNVSMVEVTDFPFNTSEWEGYLPKESIRT KAGPWGRCAVVSSAGSLKSSQLGREIDDHDAVLRFNGAPTANFQQDVGTK TTIRLMNSQLVTTEKRFLKDSLYNEGILIVWDPSVYHSDIPKWYQNPDYN FFNNYKTYRKLHPNQPFYILKPQMPWELWDILQEISPEEIQPNPPSSGML GIIIMMTLCDQVDIYEFLPSKRKTDVCYYYQKFFDSACTMGAYHPLLYEK NLVKHLNQGTDEDIYLLGKATLPGFRTIHCVDHHHHHH
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Molecular Weight
45 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
The ST6GAL1 gene encodes the enzyme ST6 beta-galactosamine alpha-2,6-sialyltransferase 1, which plays a crucial role in the sialylation of glycoproteins and glycosphingolipids. This enzymatic process is vital for various biological functions, including cell signaling, immune response, and cell-cell interactions. Abnormal ST6GAL1 activity has been implicated in several diseases, including cancer, where altered sialylation patterns can affect tumor progression and metastasis by influencing cancer cell behaviors and evasion of immune surveillance. Studies have shown that overexpression of ST6GAL1 can enhance the sialylation of glycoproteins, which may contribute to tumor aggressiveness. Consequently, understanding the structure and function of ST6GAL1 through recombinant protein studies is essential for elucidating its biological roles and potential therapeutic applications. Recombinant ST6GAL1 proteins can be utilized to investigate enzyme kinetics, substrate specificity, and the effects of various biochemical factors on sialylation processes. Additionally, these studies may lead to the development of novel biomarkers and therapeutic targets for diseases associated with aberrant sialylation. Overall, the research on ST6GAL1 recombinant proteins holds promise for advancing our knowledge of glycosylation mechanisms in health and disease, paving the way for innovative approaches in diagnostics and treatments.
