Analytical Data
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Gene name
B4GALT5
- Application
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Alternative Names
B4galt5; B4GT5_HUMAN; Beta 1 4 galactosyltransferase 5
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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
O43286
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Expression Region
1-388aa
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AA Sequence
MRARRGLLRLPRRSLLAALFFFSLSSSLLYFVYVAPGIVNTYLFMMQAQGILIRDNVRTIGAQVYEQVLRSAYAKRNSSVNDSDYPLDLNHSETFLQTTTFLPEDFTYFANHTCPERLPSMKGPIDINMSEIGMDYIHELFSKDPTIKLGGHWKPSDCMPRWKVAILIPFRNRHEHLPVLFRHLLPMLQRQRLQFAFYVVEQVGTQPFNRAMLFNVGFQEAMKDLDWDCLIFHDVDHIPESDRNYYGCGQMPRHFATKLDKYMYLLPYTEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVQNAGYSVSRPEGDTGKYKSIPHHHRGEVQFLGRYALLRKSKERQGLDGLNNLNYFANITYDALYKNITVNLTPELAQVNEY
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Molecular Weight
45.1 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
B4GALT5, also known as Beta-1,4-galactosyltransferase 5, is an enzyme involved in the glycosylation of proteins and lipids, playing a crucial role in the synthesis of complex carbohydrate structures, particularly in the formation of polysaccharides such as glycoproteins and glycolipids. Its primary function is to transfer galactose from UDP-galactose to the acceptor substrates, thereby influencing various biological processes including cell adhesion, signaling, and immune response. Dysregulation or mutations in B4GALT5 have been linked to several pathological conditions, including cancer and congenital disorders, highlighting its potential as a biomarker and therapeutic target. Research into recombinant B4GALT5 proteins facilitates a better understanding of its structure-function relationships and biochemical mechanisms, providing insights into its role in cellular processes. Such studies are essential to explore the implications of B4GALT5 in disease mechanisms and therapeutic applications, particularly in glyco-engineering and drug development. By producing and characterizing recombinant B4GALT5, researchers can elucidate its enzymatic properties, substrate specificity, and regulatory mechanisms, paving the way for novel interventions that manipulate glycosylation pathways in various diseases. Overall, the investigation of B4GALT5 holds significant promise for advancing our knowledge in glycoscience and developing innovative strategies for treating glycosylation-related disorders.
