Analytical Data
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Gene name
B4GALNT1
- Application
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Alternative Names
Beta-1.4 N-acetylgalactosaminyltransferase 1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q00973
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Expression Region
1-328aa
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AA Sequence
MWLGRRALCALVLLLACASLGLLYASTRDAPGLRLPLAPWAPPQSPRRPELPDLAPEPRYAHIPVRIKEQVVGLLAWNNCSCESSGGGLPLPFQKQVRAIDLTKAFDPAELRAASATREQEFQAFLSRSQSPADQLLIAPANSPLQYPLQGVEVQPLRSILVPGLSLQAASGQEVYQVNLTASLGTWDVAGEVTGVTLTGEGQADLTLVSPGLDQLNRQLQLVTYSSRSYQTNTADTGARPGWRDGQAGQTEKNQKGWSGQMAEGMGGIWAMARAVQPHNGCFNWTSRARGRKGAFVHLGLEQARGKPEPWVCLPFRPTVGGPRKRLV
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Molecular Weight
61.9 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
Related Products
Protein Description
B4GALNT1, known as Beta-1,4-N-acetylgalactosaminyltransferase 1, is an important glycosyltransferase enzyme involved in the biosynthesis of glycosphingolipids and glycoproteins. It catalyzes the addition of N-acetylgalactosamine (GalNAc) to specific acceptor substrates, playing a pivotal role in the formation of glycan structures that are crucial for cellular interactions, signaling, and immunological responses. Abnormalities in B4GALNT1 expression and function have been associated with various pathological conditions, including cancer and congenital disorders. Due to its significant role in cellular processes, researchers are interested in studying B4GALNT1 for potential therapeutic applications. The production of recombinant B4GALNT1 facilitates detailed investigations into its enzymatic activity, substrate specificity, and regulatory mechanisms. This research can contribute to a better understanding of its biological functions and the development of targeted strategies for disease intervention, particularly in the context of glycan-related diseases. Additionally, exploring the structural and functional aspects of B4GALNT1 through recombinant protein studies could shed light on its interactions with other biomolecules, enhancing our knowledge of glycosylation pathways and their implications in health and disease.
