Analytical Data
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Gene name
B4GALT4
- Application
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Alternative Names
B4GALT4；UGALT；UGT；UGTL；UDP-galactose translocator
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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
O60513
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Expression Region
39-344aa
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AA Sequence
QEIPKAKEFMANFHKTLILGKGKTLTNEASTKKVELDNCPSVSPYLRGQS KLIFKPDLTLEEVQAENPKVSRGRYRPEECKALQRVAILVPHRNREKHLM YLLEHLHPFLQRQQLDYGIYVIHQAEGKKFNRAKLLNVGYLEALKEENWD CFIFHDVDLVPENDFNLYKCEEHPKHLVVGRNSTGYRLRYSGYFGGVTAL SREQFFKVNGFSNNYWGWGGEDDDLRLRVELQRMKISRPLPEVGKYTMVF HTRDKGNEVNAERMKLLHQVSRVWRTDGLSSCSYKLVSVEHNPLYINITV DFWFGA
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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
B4GALT4, or Beta-1,4-galactosyltransferase 4, is an enzyme that plays a crucial role in the synthesis of glycoproteins and glycolipids by catalyzing the transfer of galactose to terminal N-acetylglucosamine residues. Its importance is underscored in various biological processes, including cell signaling, adhesion, and immune responses. Aberrant expression or mutations in B4GALT4 have been implicated in several metabolic and developmental disorders, highlighting the necessity for understanding its function and regulation. Recent studies have focused on the enzyme's structure and mechanism, aiming to elucidate the specific pathways it influences and its interactions with substrate molecules. Recombinant B4GALT4 proteins have been developed to investigate these aspects further, providing valuable insights into glycosylation patterns critical for cellular function. Additionally, research into B4GALT4 could pave the way for novel therapeutic strategies targeting glycosylation-related diseases, as enhanced knowledge of its enzymatic properties may lead to innovations in drug design and biotechnological applications. Overall, the study of B4GALT4 and its recombinant forms represents a significant advancement in the field of glycoscience, with the potential to address vital questions regarding carbohydrate metabolism and its associated pathological conditions.
