Analytical Data
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Gene name
b4GALNT2
- Application
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Alternative Names
SD; B4GALGT2; B4GALT; Cad; GALGT2; Sda; Sd(a) beta-1,4-GalNAc transferase; UDP-GalNAc:Neu5Aca2-3Galb-R b1,4-N-acetylgalactosaminyltransferase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8NHY0
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Expression Region
Thr324~Ala566
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Molecular Weight
31kDa
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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
B4GALNT2, or beta-1,4-N-acetylgalactosaminyltransferase 2, plays a critical role in glycan biosynthesis, particularly in the formation of glycosaminoglycans and glycoproteins. This enzyme is integral to the addition of N-acetylgalactosamine (GalNAc) residues to various molecular substrates, influencing multiple biological processes, including cell-cell adhesion, signaling, and differentiation. Mutations in the B4GALNT2 gene have been linked to several developmental disorders, highlighting its importance in human health. Given its significant role in glycosylation pathways, research focuses on the characterization and functional analysis of B4GALNT2 recombinant protein. By producing and studying this protein, scientists aim to elucidate its mechanism of action, substrate specificity, and potential therapeutic applications. Understanding B4GALNT2 can provide insights into disease mechanisms and facilitate the development of targeted therapies for conditions related to defective glycosylation. The study of recombinant B4GALNT2 is thus a vital step toward harnessing its potential in biotechnology and medicine, offering pathways for innovation in treatment strategies for glycosylation-related disorders.
