Analytical Data
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Gene name
b3GAT2
- Application
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Alternative Names
b3GAT2；GLCATS；KIAA1963；GalactosylgalactosylxylosylProtein 3-beta-glucuronosyltransferase 2
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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
Q9NPZ5
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Expression Region
1-323aa
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AA Sequence
MKSALFTRFFILLPWILIVIIMLDVDTRRPVPPLTPRPYFSPYAVGRGGARLPLRRGGPAHGTQKRNQSRPQPQPEPQLPTIYAITPTYSRPVQKAELTRLANTFRQVAQLHWILVEDAAARSELVSRFLARAGLPSTHLHVPTPRRYKRPGLPRATEQRNAGLAWLRQRHQHQRAQPGVLFFADDDNTYSLELFQEMRTTRKVSVWPVGLVGGRRYERPLVENGKVVGWYTGWRADRPFAIDMAGFAVSLQVILSNPKAVFKRRGSQPGMQESDFLKQITTVEELEPKANNCTKVLVWHTRTEKVNLANEPKYHLDTVKIEV
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Molecular Weight
36.9 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
B3GAT2, or Beta-1,3-Galactosyltransferase 2, is an enzyme involved in glycosylation, a critical post-translational modification process that influences protein stability, folding, and function. Glycosylation plays an essential role in various biological processes, including cell signaling, immune response, and cell adhesion. Recent studies have shown that B3GAT2 is implicated in the biosynthesis of glycosaminoglycans, particularly in the formation of proteoglycans, which are vital components of the extracellular matrix. Aberrant expression or dysfunction of B3GAT2 has been linked to several pathological conditions, including developmental disorders and cancer, highlighting its significance in cellular biology and disease. The recombinant expression and study of B3GAT2 can provide insights into its functional mechanisms, potential regulatory pathways, and interactions with other glycosylation-related enzymes. Understanding the structure and activity of this enzyme can lead to the development of therapeutic approaches targeting glycosylation anomalies and contribute to advances in regenerative medicine, cancer therapy, and biotechnology. Therefore, research on B3GAT2 is crucial for elucidating the complex roles of glycosylation in health and disease, paving the way for novel diagnostic and therapeutic strategies.
