关键信息
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基因名
FNTa
- 应用
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别名
FNTa；Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
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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
P49354
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表达区间
2-379aa
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氨基酸序列
AATEGVGEA AQGGEPGQPA QPPPQPHPPP PQQQHKEEMA AEAGEAVASP MDDGFVSLDS PSYVLYRDRA EWADIDPVPQ NDGPNPVVQI IYSDKFRDVY DYFRAVLQRD ERSERAFKLT RDAIELNAAN YTVWHFRRVL LKSLQKDLHE EMNYITAIIE EQPKNYQVWH HRRVLVEWLR DPSQELEFIA DILNQDAKNY HAWQHRQWVI QEFKLWDNEL QYVDQLLKED VRNNSVWNQR YFVISNTTGY NDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS KYPNLLNQLL DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT IRKEYWRYIG RSLQSKHSTE NDSPTNVQQ
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分子量
44.4 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.
质检流程
相关产品
背景信息
The study of FNTa recombinant protein is rooted in the growing interest in understanding protein functions and their applications in biotechnology and medicine. FNTa, a specific recombinant protein, has garnered attention due to its unique structural properties and potential role in various biological processes. Researchers have identified FNTa's involvement in cellular signaling and its potential as a therapeutic target in diseases such as cancer and metabolic disorders. The production of FNTa through recombinant DNA technology allows for the generation of large quantities of this protein, facilitating detailed functional studies and enabling the exploration of its interactions with other biomolecules. This approach not only improves our understanding of FNTa's biological significance but also opens avenues for developing novel diagnostic and therapeutic strategies. Furthermore, the study of FNTa can enhance our knowledge of protein engineering and synthetic biology, contributing to advancements in drug delivery systems and vaccine development. Thus, the investigation of FNTa recombinant protein represents a crucial intersection of fundamental research and practical applications, with the potential to significantly impact health and disease management.
