Analytical Data
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基因名
FUT9
- Application
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别名
4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9. EC:2.4.1.152. Fucosyltransferase 9
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9Y231
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表达区间
1-359aa
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氨基酸序列
MTSTSKGILRPFLIVCIILGCFMACLLIYIKPTNSWIFSPMESASSVLKMKNFFSTKTDYFNETTILVWVWPFGQTFDLTSCQAMFNIQGCHLTTDRSLYNKSHAVLIHHRDISWDLTNLPQQARPPFQKWIWMNLESPTHTPQKSGIEHLFNLTLTYRRDSDIQVPYGFLTVSTNPFVFEVPSKEKLVCWVVSNWNPEHARVKYYNELSKSIEIHTYGQAFGEYVNDKNLIPTISACKFYLSFENSIHKDYITEKLYNAFLAGSVPVVLGPSRENYENYIPADSFIHVEDYNSPSELAKYLKEVDKNNKLYLSYFNWRKDFTVNLPRFWESHACLACDHVKRHQEYKSVGNLEKWFWN
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分子量
68.4 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.
