Analytical Data
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基因名
HYOU1
- Application
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别名
HYOU1; HSP12A; Grp170; Glucose-Regulated Protein 170; Hypoxia Up Regulated 1
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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
Q9Y4L1
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表达区间
Met695~Leu994
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分子量
44kDa
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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
HYOU1, also known as hypoxia up-regulated 1, is a protein that has garnered significant attention in the field of molecular biology and medicine due to its role in cellular response to stress, particularly in hypoxic conditions. This protein is associated with the endoplasmic reticulum (ER) and plays a crucial role in protein folding and cellular homeostasis. Research has demonstrated that HYOU1 is upregulated in various pathological conditions, including cancer, where it contributes to tumor growth and survival by enhancing the adaptability of cancer cells to hypoxic environments. Moreover, HYOU1 is thought to be involved in the regulation of the unfolded protein response (UPR), a protective mechanism activated under stress conditions that aims to restore normal cell function. This makes HYOU1 a potential target for therapeutic strategies aimed at modulating the UPR in diseases characterized by hypoxia or enhanced ER stress. The study of HYOU1 as a recombinant protein allows for a deeper understanding of its structure, function, and interactions within the cell, potentially leading to novel approaches in cancer treatment and other diseases where hypoxic conditions prevail. Given its importance in both normal physiology and disease pathology, ongoing research into the functional mechanisms of HYOU1 and its potential applications in clinical settings is vital for the advancement of therapeutic interventions.
