Analytical Data
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Gene name
FUT4
- Application
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Alternative Names
FUT4；ELFT；FCT3A；Alpha-(1.3)-fucosyltransferase 4
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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
P22083
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Expression Region
167-265aa
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AA Sequence
ITYACWGQLPPLPWASPTPSRPVGVLLWWEPFGGRDSAPRPPPDCRLRFN ISGCRLLTDRASYGEAQAVLFHHRDLVKGPPDWPPPWGIQAHTAEEVDL
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Molecular Weight
37 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
FUT4, or fucosyltransferase 4, is an important enzyme that catalyzes the addition of fucose, a hexose sugar, to glycoproteins and glycolipids, playing a crucial role in cellular processes such as cell adhesion, immune response, and signaling. Its significance has garnered attention in various fields, including immunology, oncology, and developmental biology, as fucosylation can influence cell behavior and disease progression. Abnormal FUT4 expression has been associated with several pathological conditions, including cancer metastasis and inflammatory diseases. Understanding the mechanisms of FUT4 activity and regulation can potentially lead to novel therapeutic strategies targeting fucosylation-related pathways. Consequently, researchers are increasingly focused on producing recombinant FUT4 proteins to study their structure and function in detail. These recombinant proteins serve as valuable tools for elucidating the role of fucosylation in biological systems and for exploring their potential as biomarkers and therapeutic targets in disease contexts. Furthermore, advancements in recombinant DNA technology facilitate the efficient production of FUT4, allowing researchers to investigate its enzymatic mechanisms, substrate specificity, and interactions with other glycosylation enzymes, thereby paving the way for enhanced understanding of glycosylation's impact on human health and disease.
