关键信息
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基因名
FUT8
- 应用
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别名
FUT8；Alpha-(1.6)-fucosyltransferase
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9BYC5
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表达区间
1-575aa
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氨基酸序列
MRPWTGSWRWIMLILFAWGTLLFYIGGHLVRDNDHPDHSSRELSKILAKL ERLKQQNEDLRRMAESLRIPEGPIDQGPAIGRVRVLEEQLVKAKEQIENY KKQTRNGLGKDHEILRRRIENGAKELWFFLQSELKKLKNLEGNELQRHAD EFLLDLGHHERSIMTDLYYLSQTDGAGDWREKEAKDLTELVQRRITYLQN PKDCSKAKKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRTLILESQNWRY ATGGWETVFRPVSETCTDRSGISTGHWSGEVKDKNVQVVELPIVDSLHPR PPYLPLAVPEDLADRLVRVHGDPAVWWVSQFVKYLIRPQPWLEKEIEEAT KKLGFKHPVIGVHVRRTDKVGTEAAFHPIEEYMVHVEEHFQLLARRMQVD KKRVYLATDDPSLLKEAKTKYPNYEFISDNSISWSAGLHNRYTENSLRGV ILDIHFLSQADFLVCTFSSQVCRVAYEIMQTLHPDASANFHSLDDIYYFG GQNAHNQIAIYAHQPRTADEIPMEPGDIIGVAGNHWDGYSKGVNRKLGRT GLYPSYKVREKIETVKYPTYPEAEK
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分子量
89 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.
质检流程
相关产品
背景信息
The FUT8 recombinant protein has garnered significant interest in the fields of glycobiology and therapeutic development due to its pivotal role in glycosylation, specifically in the fucosylation of glycoproteins. Fucosylation is an essential post-translational modification that influences protein stability, immune recognition, and cell signaling, making it crucial for various biological processes and disease mechanisms. Aberrant fucosylation is associated with several pathological conditions, including cancer, inflammatory diseases, and infectious diseases, highlighting the importance of understanding FUT8's function. As a key enzyme, FUT8 catalyzes the addition of fucose residues to specific glycan structures, which can alter cell behavior and messaging within the immune system. Current research aims to elucidate the structural and functional characteristics of FUT8, employing recombinant expression systems to produce functional FUT8 proteins for biochemical and biophysical studies. These investigations are critical for delineating the enzyme's mechanism of action, its role in health and disease, and its potential as a therapeutic target. Furthermore, the recombinant FUT8 protein may facilitate the development of novel glyco-engineered biopharmaceuticals, enabling enhanced efficacy and reduced immunogenicity due to optimized glycosylation patterns. As such, FUT8 represents a promising area of study within glycoengineering and personalized medicine, with the potential to unlock new avenues for disease intervention and treatment.
