Analytical Data
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Gene name
b3GNT3
- Application
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Alternative Names
b3GNT3；B3GALT8；TMEM3；N-acetyllactosaminide beta-1.3-N-acetylglucosaminyltransferase 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
Q9Y2A9
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Expression Region
1-372aa
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AA Sequence
MKYLRHRRPNATLILAIGAFTLLLFSLLVSPPTCKVQEQPPAIPEALAWPTPPTRPAPAPCHANTSMVTHPDFATQPQHVQNFLLYRHCRHFPLLQDVPPSKCAQPVFLLLVIKSSPSNYVRRELLRRTWGRERKVRGLQLRLLFLVGTASNPHEARKVNRLLELEAQTHGDILQWDFHDSFFNLTLKQVLFLQWQETRCANASFVLNGDDDVFAHTDNMVFYLQDHDPGRHLFVGQLIQNVGPIRAFWSKYYVPEVVTQNERYPPYCGGGGFLLSRFTAAALRRAAHVLDIFPIDDVFLGMCLELEGLKPASHSGIRTSGVRAPSQRLSSFDPCFYRDLLLVHRFLPYEMLLMWDALNQPNLTCGNQTQIY
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Molecular Weight
42.5 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
b3GNT3, or Beta-1,3-N-acetylglucosaminyltransferase 3, is an enzyme critically involved in glycosylation processes, specifically in the biosynthesis of complex glycan structures on glycoproteins and glycolipids. Its function primarily relates to the transfer of N-acetylglucosamine (GlcNAc) residues to acceptor molecules, which plays a significant role in various biological processes, including cell signaling, adhesion, and immune responses. Aberrations in glycosylation, often due to the dysfunction of glycosyltransferases like b3GNT3, have been associated with various diseases, including cancers and congenital disorders. As such, studying the recombinant expression of b3GNT3 offers valuable insights into its functional role and potential therapeutic applications. Protein engineering techniques can be utilized to produce b3GNT3 in substantial quantities, enabling detailed characterization of its activity, substrate specificity, and interaction with other biomolecules. Furthermore, understanding the regulatory mechanisms governing b3GNT3 expression and activity could open avenues for targeted drug development or enzyme replacement therapies, providing hope for conditions arising from glycosylation defects. The ongoing research into b3GNT3 underscores its importance not only in fundamental biological research but also in clinical applications, highlighting the potential for interventions that modulate glycan biosynthesis pathways.
