Analytical Data
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Gene name
B3GNT7
- Application
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8NFL0
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Expression Region
27-401aa
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Molecular Weight
50.5 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
B3GNT7, or Beta-1,3-N-acetylglucosaminyltransferase 7, is an enzyme that plays a critical role in the biosynthesis of glycoproteins and glycolipids by catalyzing the transfer of N-acetylglucosamine (GlcNAc) residues to specific substrates. Its function is particularly significant in the formation of complex carbohydrate structures, including branched N-glycans and specific glycan motifs that are essential for cell signaling, immune responses, and developmental processes. Research into B3GNT7 has gained momentum due to its implications in various biological processes and disease states, including cancer metastasis, where altered glycosylation patterns can influence tumor cell behavior and immune evasion mechanisms. Furthermore, aberrant expression of B3GNT7 has been linked to certain pathological conditions, highlighting its potential as a therapeutic target or biomarker. The production and characterization of recombinant B3GNT7 proteins allow for detailed investigation of its enzymatic properties, substrate specificity, and regulatory mechanisms, which are crucial for understanding its role in health and disease. Advances in recombinant DNA technology and protein expression systems have facilitated the purification and functional analysis of B3GNT7, paving the way for novel insights into its contribution to glycan diversity and its potential applications in biomedical research. As researchers continue to unravel the complexities of glycosylation, B3GNT7 stands out as a significant player in the intricate network of cellular interactions and functions, making it a valuable focus for continued exploration in glycobiology.
