Analytical Data
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基因名
EIF4EBP1
- Application
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别名
EIF4EBP1；EIF4EL1；EIF4F;Eukaryotic translation initiation factor 4E
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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
Q13541
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表达区间
2-118aa
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氨基酸序列
SGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI
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分子量
19.4kDa
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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
EIF4EBP1, also known as eukaryotic translation initiation factor 4E-binding protein 1, plays a crucial role in the regulation of protein synthesis and cell growth by interacting with the translation initiation factor 4E. This protein is a key player in the mTOR (mechanistic target of rapamycin) signaling pathway, which is known to influence various cellular processes, including metabolism, growth, and proliferation. Dysregulation of EIF4EBP1 has been implicated in several diseases, including cancer and neurodegenerative disorders, making it a significant target for research. Understanding the structure and function of recombinant EIF4EBP1 can provide insights into its regulatory mechanisms and interactions with other cellular proteins. Moreover, the study of its phosphorylation state, which regulates its binding affinity for EIF4E, can shed light on how cells adapt to different growth conditions and stresses. By employing recombinant DNA technology, researchers can produce EIF4EBP1 in vitro, allowing for detailed biochemical studies and potential therapeutic developments. This research not only enhances our knowledge of translation regulation but also opens avenues for developing novel strategies to manipulate protein synthesis in various disease contexts, contributing to advancements in targeted therapies.
