Analytical Data
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Gene name
B3GAT3
- Application
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Alternative Names
GLCATI; GlcAT-I; Glucuronosyltransferase I; Galactosylgalactosylxylosylprotein 3-Beta-Glucuronosyltransferase 3; UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase
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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 95% as determined by SDS-PAGE.
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Uniprot
O94766
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Expression Region
Leu74~Val335
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Molecular Weight
33kDa
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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
B3GAT3 (beta-1,3-glucuronyltransferase 3) is an enzyme that plays a crucial role in glycosaminoglycan biosynthesis, particularly in the synthesis of dermatan sulfate and heparan sulfate. These glycosaminoglycans are essential components of the extracellular matrix, influencing various biological processes, including cell signaling, growth, and development. Mutations in the B3GAT3 gene have been associated with several rare genetic disorders, such as the Ehlers-Danlos syndrome and other connective tissue disorders, marking its importance in human health. Understanding the structure and function of B3GAT3 at the molecular level is vital for elucidating its role in these diseases and for potential therapeutic interventions. Recent advances in recombinant protein technology have enabled researchers to produce B3GAT3 in heterologous systems. This has allowed for detailed studies of its enzymatic activity and interactions with donor and acceptor substrates, providing insights into its catalytic mechanisms. Furthermore, the study of B3GAT3’s role in glycan biosynthesis can lead to better comprehension of various pathological conditions related to glycosylation defects. By characterizing the recombinant B3GAT3 protein, researchers aim to develop targeted therapies that can address the underlying biochemical abnormalities associated with B3GAT3-related disorders, paving the way for novel treatments and improved patient outcomes. The continued exploration of this enzyme holds the promise of advancing our understanding of glycosaminoglycan function and the molecular underpinnings of connective tissue diseases, ultimately contributing to the broader field of glycobiology and its therapeutic applications.
