Analytical Data
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Gene name
B3GNT1
- Application
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Alternative Names
B4GAT1; B3GNT1; B3GNT6; Beta-1.4-glucuronyltransferase 1
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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
O43505
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Expression Region
1-415aa
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AA Sequence
MQMSYAIRCAFYQLLLAALMLVAMLQLLYLSLLSGLHGQEEQDQYFEFFPPSPRSVDQVKAQLRTALASGGVLDASGDYRVYRGLLKTTMDPNDVILATHASVDNLLHLSGLLERWEGPLSVSVFAATKEEAQLATVLAYALSSHCPDMRARVAMHLVCPSRYEAAVPDPREPGEFALLRSCQEVFDKLARVAQPGINYALGTNVSYPNNLLRNLAREGANYALVIDVDMVPSEGLWRGLREMLDQSNQWGGTALVVPAFEIRRARRMPMNKNELVQLYQVGEVRPFYYGLCTPCQAPTNYSRWVNLPEESLLRPAYVVPWQDPWEPFYVAGGKVPTFDERFRQYGFNRISQACELHVAGFDFEVLNEGFLVHKGFKEALKFHPQKEAENQHNKILYRQFKQELKAKYPNSPRRC
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Molecular Weight
47.1 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 glycan biosynthesis, specifically in the synthesis of O-glycans, which play critical roles in cell signaling, protein stability, and cellular interactions. Alterations in glycosylation patterns can lead to various diseases, including cancer and congenital disorders. Research into the B3GNT1 recombinant protein has gained significant attention due to its potential implications in therapeutic development and disease understanding. The recombinant production of B3GNT1 allows for detailed structural and functional studies, facilitating insights into its catalytic mechanisms and substrate specificity. Furthermore, understanding B3GNT1's role in glycan formation could offer novel targets for drug development and strategies for modulating glycosylation patterns in therapeutic contexts. Enhanced knowledge of B3GNT1 may lead to breakthroughs in diagnostic and treatment approaches for diseases associated with aberrant glycosylation, highlighting its importance in both basic and applied biomedical research.
