Analytical Data
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Gene name
B3GAT3
- Application
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Alternative Names
B3GAT3；GalactosylgalactosylxylosylProtein 3-beta-glucuronosyltransferase 3
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O94766
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Expression Region
29-335aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSQPCDCLPPLRAAAEQLRQKDLRISQLQ AELRRPPPAPAQPPEPEALPTIYVVTPTYARLVQKAELVRLSQTLSLVPR LHWLLVEDAEGPTPLVSGLLAASGLLFTHLVVLTPKAQRLREGEPGWVHP RGVEQRNKALDWLRGRGGAVGGEKDPPPPGTQGVVYFADDDNTYSRELFE EMRWTRGVSV WPVGLVGGLR FEGPQVQDGRVVGFHTAWEPSRPFPVDMAGFAVALPLLLDKPNAQFDSTA PRGHLESSLLSHLVDPKDLEPRAANCTRVLVWHTRTEKPKMKQEEQLQRQ GRGSDPAIEV
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Molecular Weight
36 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
B3GAT3, or Beta-1,3-glucuronyltransferase 3, is a significant enzyme that plays a crucial role in glycosaminoglycan (GAG) biosynthesis, specifically in the synthesis of heparan sulfate and related polysaccharides. Alterations in B3GAT3 function have been implicated in various developmental and pathological conditions, including congenital disorders and cancers. The enzyme catalyzes the attachment of glucuronic acid to glycoproteins and proteoglycans, influencing cellular interactions, signaling pathways, and extracellular matrix composition. Research on B3GAT3 has expanded in recent years, uncovering its involvement in modulating cellular processes such as proliferation, differentiation, and migration. Understanding the regulation and mechanism of B3GAT3 could provide insights into therapeutic approaches for diseases characterized by GAG imbalances. Additionally, the study of this enzyme offers potential applications in regenerative medicine and tissue engineering, where the modulation of glycosylation patterns is crucial for the development of functional biomaterials. Despite its physiological significance, the molecular pathways and regulatory networks involving B3GAT3 remain poorly understood, warranting further investigation to elucidate its overall role in health and disease.
