Analytical Data
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Gene name
ST6GALNAC6
- Application
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Alternative Names
ST6GALNAC6; SIAT7F; UNQ708/PRO1359; Alpha-N-acetylgalactosaminide alpha-2.6-sialyltransferase 6; EC 2.4.99.-; GalNAc alpha-2.6-sialyltransferase VI; ST6GalNAc VI; ST6GalNAcVI; hST6GalNAc VI; Sialyltransferase 7F; SIAT7-F
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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
Q969X2
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Expression Region
1-333 aa
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AA Sequence
MACSRPPSQCEPTSLPPGPPAGRRHLPLSRRRREMSSNKEQRSAVFVILFALITILILYSSNSANEVFHYGSLRGRSRRPVNLKKWSITDGYVPILGNKTLPSRCHQCVIVSSSSHLLGTKLGPEIERAECTIRMNDAPTTGYSADVGNKTTYRVVAHSSVFRVLRRPQEFVNRTPETVFIFWGPPSKMQKPQGSLVRVIQRAGLVFPNMEAYAVSPGRMRQFDDLFRGETGKDREKSHSWLSTGWFTMVIAVELCDHVHVYGMVPPNYCSQRPRLQRMPYHYYEPKGPDECVTYIQNEHSRKGNHHRFITEKRVFSSWAQLYGITFSHPSWT
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Molecular Weight
62.37 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
ST6GALNAC6, a member of the ST6GalNAc family of sialyltransferases, plays a pivotal role in the biosynthesis of sialylated glycoproteins and glycolipids by catalyzing the transfer of sialic acid to N-acetylgalactosamine (GalNAc) residues. The enzyme's activity is crucial for modulating cell surface glycoconjugates, which significantly influence cellular interactions, signaling pathways, and immune responses. Dysregulation of ST6GALNAC6 expression has been implicated in various diseases, including cancer, where aberrant sialylation contributes to tumor progression and metastasis. Consequently, understanding the structure and function of ST6GALNAC6 is vital for elucidating its biological roles and potential as a therapeutic target. Recent advances in recombinant protein technology facilitate the expression and purification of ST6GALNAC6, enabling detailed studies of its enzymatic properties, substrate specificity, and regulatory mechanisms. Such research not only enhances our comprehension of sialylation processes but also opens avenues for innovative strategies in cancer treatment and other sialylation-related disorders.
