Analytical Data
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基因名
IRE1
- Application
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别名
IRE1; IRE1P; Serine/Threonine-Protein Kinase/Endoribonuclease IRE1; Inositol-requiring protein 1; Ire1-alpha; Serine/threonine-protein kinase; Endoribonuclease
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种属
Human
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
O75460
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表达区间
Phe571~Phe832
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分子量
36kDa
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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
Related Products
Protein Description
IRE1 (Inositol-requiring enzyme 1) is a critical component of the unfolded protein response (UPR), a cellular stress response activated by the accumulation of misfolded proteins in the endoplasmic reticulum (ER). Research on IRE1 has gained significant attention due to its dual role as a sensor of ER stress and as an endoribonuclease that regulates the splicing of X-box binding protein 1 (XBP1), ultimately influencing cell survival and apoptosis. Dysregulation of IRE1 activity is implicated in various diseases, including neurodegenerative disorders, diabetes, and cancer, making it a potential therapeutic target. Recent studies have explored the structural and functional aspects of IRE1, revealing its complex regulation and the potential for pharmacological modulation. Additionally, the development of recombinant IRE1 proteins has facilitated the investigation of its mechanisms at a molecular level, enhancing our understanding of how it contributes to cellular homeostasis under stress conditions. As research progresses, the therapeutic implications of modulating IRE1 activity in disease contexts are becoming increasingly salient.
