Analytical Data
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Gene name
B3GNT4
- Application
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Alternative Names
B3GNT4; UNQ1898/PRO4344N-acetyllactosaminide beta-1.3-N-acetylglucosaminyltransferase 4
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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
Q9C0J1
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Expression Region
1-378aa
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AA Sequence
MLPPQPSAAHQGRGGRSGLLPKGPAMLCRLCWLVSYSLAVLLLGCLLFLRKAAKPAGDPTAHQPFWAPPTPRHSRCPPNHTVSSASLSLPSRHRLFLTYRHCRNFSILLEPSGCSKDTFLLLAIKSQPGHVERRAAIRSTWGRVGGWARGRQLKLVFLLGVAGSAPPAQLLAYESREFDDILQWDFTEDFFNLTLKELHLQRWVVAACPQAHFMLKGDDDVFVHVPNVLEFLDGWDPAQDLLVGDVIRQALPNRNTKVKYFIPPSMYRATHYPPYAGGGGYVMSRATVRRLQAIMEDAELFPIDDVFVGMCLRRLGLSPMHHAGFKTFGIRRPLDPLDPCLYRGLLLVHRLSPLEMWTMWALVTDEGLKCAAGPIPQR
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Molecular Weight
42.3 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
B3GNT4, or Beta-1,3-N-acetylglucosaminyltransferase 4, is an essential glycosyltransferase involved in the synthesis of glycosaminoglycans, specifically in the formation of heparan sulfate and other carbohydrate structures that play critical roles in various biological processes. Research into B3GNT4 is significant as these glycan chains are crucial for cell signaling, proliferation, differentiation, and the maintenance of cellular architecture. Dysregulation of glycosylation patterns, including those mediated by B3GNT4, has been implicated in various pathological conditions, including cancer, developmental disorders, and inflammatory diseases. Consequently, understanding the structure and function of B3GNT4, along with developing recombinant forms of this protein, has become a focus of scientific inquiry. By elucidating the enzymatic activity and substrate specificity of B3GNT4, researchers aim to uncover its role in disease mechanisms and potentially leverage this knowledge for therapeutic applications. The production of recombinant B3GNT4 allows for detailed biochemical studies, enabling insights into its catalytic properties and interactions with other proteins, thereby contributing to a more comprehensive understanding of glycosylation processes and their implications in health and disease.
