Analytical Data
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Gene name
B3GNT1
- Application
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Alternative Names
rHuB3GNT1, His; B3GNT1; Beta-1,3-N-Acetylglucosaminyltransferase 1;
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Species
Human
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Source
HEK293
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Tag
C-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43505
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Expression Region
D43-C415
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AA Sequence
DQYFEFFPPSPRSVDQVKAQLRTALASGGVLDASGDYRVYRGLLKTTMDPNDVILATHASVDNLLHLSGLLERWEGPLSVSVFAATKEEAQLATVLAYALSSHCPDMRARVAMHLVCPSRYEAAVPDPREPGEFALLRSCQEVFDKLARVAQPGINYALGTNVSYPNNLLRNLAREGANYALVIDVDMVPSEGLWRGLREMLDQSNQWGGTALVVPAFEIRRARRMPMNKNELVQLYQVGEVRPFYYGLCTPCQAPTNYSRWVNLPEESLLRPAYVVPWQDPWEPFYVAGGKVPTFDERFRQYGFNRISQACELHVAGFDFEVLNEGFLVHKGFKEALKFHPQKEAENQHNKILYRQFKQELKAKYPNSPRRCHHHHHH
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Protein Length
Partial
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Molecular Weight
45-55 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
B3GNT1, or Beta-1,3-N-acetylglucosaminyltransferase 1, is an essential enzyme involved in glycosylation, specifically in the synthesis of complex carbohydrates on glycoproteins and glycolipids. Its primary function is to transfer N-acetylglucosamine to specific acceptor substrates, playing a pivotal role in the formation of various glycan structures, which are crucial for numerous biological processes, including cell-cell communication, immune response, and tissue development. Aberrant expression of B3GNT1 has been linked to several pathological conditions, including cancer and congenital disorders. Understanding its structure, function, and regulation can provide insights into its potential as a therapeutic target. Recent advances in recombinant protein technology have enabled the production of B3GNT1 in sufficient quantities for in vitro studies, facilitating detailed investigations into its enzymatic mechanism and substrate specificity. Such studies are essential for unraveling the biological significance of B3GNT1 and its role in health and disease, paving the way for future therapeutic applications and biomarker development.
