Analytical Data
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Gene name
b3GALT1
- Application
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Alternative Names
b3GALT1；Beta-1.3-galactosyltransferase 1
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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
Q9Y5Z6
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Expression Region
1-326aa
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AA Sequence
MASKVSCLYVLTVVCWASALWYLSITRPTSSYTGSKPFSHLTVARKNFTFGNIRTRPINPHSFEFLINEPNKCEKNIPFLVILISTTHKEFDARQAIRETWGDENNFKGIKIATLFLLGKNADPVLNQMVEQESQIFHDIIVEDFIDSYHNLTLKTLMGMRWVATFCSKAKYVMKTDSDIFVNMDNLIYKLLKPSTKPRRRYFTGYVINGGPIRDVRSKWYMPRDLYPDSNYPPFCSGTGYIFSADVAELIYKTSLHTRLLHLEDVYVGLCLRKLGIHPFQNSGFNHWKMAYSLCRYRRVITVHQISPEEMHRIWNDMSSKKHLRC
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Molecular Weight
37.9 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
B3GALT1, or Beta-1,3-Galactosyltransferase 1, is an essential enzyme in the glycosylation process, responsible for synthesizing polysaccharides and glycoproteins. Specifically, it catalyzes the transfer of galactose to specific acceptor molecules, which is crucial for the formation of carbohydrate structures in cells, influencing cell recognition, signaling, and overall metabolic processes. Research into B3GALT1 has gained prominence due to its implications in various pathological conditions, including congenital disorders of glycosylation, cancer progression, and cardiovascular diseases. Understanding the biochemical mechanisms of B3GALT1 and the functional consequences of its activity can provide insights into disease mechanisms and potential therapeutic targets. Additionally, the recombinant production of B3GALT1 protein enables the study of its enzymatic properties, substrate specificity, and interaction with other cellular components. This research not only enhances our understanding of glycosylation but also paves the way for developing novel strategies in biotechnology and medicine, including drug design and regenerative therapies. As scientists continue to explore the role of B3GALT1 in health and disease, the emphasis on producing and characterizing this recombinant protein is crucial for advancing our knowledge in cellular biology and providing potential avenues for therapeutic interventions.
