Analytical Data
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Gene name
b3GNT3
- Application
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Alternative Names
B3GAL-T8; B3GN-T3; B3GNT-3; TMEM3; beta3Gn-T3; Putative Type II Membrane Protein; Transmembrane Protein 3; Core 1 extending beta-1,3-N-acetylglucosaminyltransferase
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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
Q9Y2A9
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Expression Region
Leu165~Arg277
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Molecular Weight
15kDa
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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
B3GNT3, a member of the glycosyltransferase family, plays a crucial role in the biosynthesis of glycosaminoglycans and glycoproteins by catalyzing the transfer of specific sugar moieties to target molecules. This enzyme is involved in the synthesis of various oligosaccharides that influence cell signaling, adhesion, and proliferation. Research on B3GNT3 has garnered attention due to its implications in developmental processes and potential links to various diseases, including cancer and diabetes. Abnormal expression levels of B3GNT3 have been associated with altered cellular behaviors that can contribute to tumor progression and metastasis. Therefore, understanding the structure, function, and regulation of B3GNT3 is essential for elucidating its biological roles and therapeutic potential. Recombinant B3GNT3 protein has been produced to facilitate this research, allowing for detailed studies of its enzymatic activities, substrate specificity, and interactions with other cellular components. These studies are pivotal for developing targeted treatments that can modulate glycosylation patterns associated with disease. Overall, the investigation of B3GNT3 not only enhances our comprehension of glycan biology but also paves the way for novel therapeutic avenues.
