Analytical Data
-
Gene name
B4GALT3
- Application
-
Alternative Names
UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 3UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 3 3 domains:N-acetyllactosamine synthase (EC:2.4.1.90) ;Nal synthaseBeta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase (EC:2.4.1.38)Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase (EC:2.4.1.-)
-
Species
Human
-
Source
E. coli
-
Tag
N- GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O60512
-
Expression Region
34-393aa
-
Molecular Weight
67.2 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
B4GALT3, or Beta-1,4-galactosyltransferase 3, is an essential enzyme in the glycosylation pathway that catalyzes the transfer of galactose to specific substrates, playing a vital role in the biosynthesis of glycoproteins and glycolipids. This enzyme is particularly important for the formation of certain glycoconjugates involved in cell-cell interaction, cellular signaling, and immune responses. Research has shown that mutations or dysregulation of B4GALT3 can lead to various pathological conditions, including congenital disorders of glycosylation and have potential implications in cancer biology due to its role in tumor progression and metastasis. The production of recombinant B4GALT3 proteins allows for in-depth functional studies, offering insights into the enzyme's mechanism and its impact on cellular functions. Characterizing B4GALT3 through recombinant protein techniques also facilitates the development of therapeutic strategies targeting glycosylation processes, aiming to correct glycosylation defects associated with genetic disorders. Consequently, investigating the structural and functional aspects of B4GALT3 is crucial for understanding its biological significance and potential as a biomarker or therapeutic target in various diseases. Through advanced biochemical and structural analysis, researchers aim to elucidate the roles of this enzyme, paving the way for innovative approaches to treat disorders linked to aberrant glycosylation.
