Analytical Data
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Gene name
FUT9
- Application
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Alternative Names
4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9. EC:2.4.1.152. Fucosyltransferase 9
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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
Q9Y231
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Expression Region
1-359aa
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AA Sequence
MTSTSKGILRPFLIVCIILGCFMACLLIYIKPTNSWIFSPMESASSVLKMKNFFSTKTDYFNETTILVWVWPFGQTFDLTSCQAMFNIQGCHLTTDRSLYNKSHAVLIHHRDISWDLTNLPQQARPPFQKWIWMNLESPTHTPQKSGIEHLFNLTLTYRRDSDIQVPYGFLTVSTNPFVFEVPSKEKLVCWVVSNWNPEHARVKYYNELSKSIEIHTYGQAFGEYVNDKNLIPTISACKFYLSFENSIHKDYITEKLYNAFLAGSVPVVLGPSRENYENYIPADSFIHVEDYNSPSELAKYLKEVDKNNKLYLSYFNWRKDFTVNLPRFWESHACLACDHVKRHQEYKSVGNLEKWFWN
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Molecular Weight
68.4 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
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Protein Description
FUT9, or fucosyltransferase 9, is a pivotal enzyme responsible for the addition of fucose residues to glycoconjugates, significantly influencing various biological processes, including cell signaling, adhesion, and immune responses. Fucosylation, the process catalyzed by FUT9, plays a crucial role in enhancing the stability and functionality of glycoproteins and glycolipids, which are essential for cellular interactions and communication. Dysregulation of fucosylation has been implicated in numerous diseases, including cancer, inflammatory conditions, and autoimmune disorders, highlighting the importance of FUT9 in health and disease. Research on FUT9 involves exploring its enzymatic activity, substrate specificity, and regulatory mechanisms, aiming to understand its biological functions and therapeutic potential. Recent advancements in recombinant protein technology have allowed for the production and characterization of FUT9, facilitating structured studies on its role in fucosylation pathways. These investigations provide valuable insights into the enzyme’s implications in pathophysiological processes, offering potential targets for novel therapeutic strategies aimed at modulating fucosylation for disease treatment. Understanding FUT9 could lead to breakthroughs in developing biomarker panels for early disease detection and targeted therapies that manipulate fucosylation processes to improve patient outcomes.
