Analytical Data
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基因名
U22
- Application
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别名
U22；EJLF1；GlycoProtein U22
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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
Q69557
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表达区间
21-202aa
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氨基酸序列
SLHIINNENSVFIATHSETELRHWLIFVKMAQRNGTAWWRMASVPINAYFERDIAFLFNPRCVIETAMGSKILCRYNKNIGVVFVDNDTKCNVSFPSGVQLQLLNQSVMESIRTKTYVVDYARKTTERGDCFISVAFCRKERRRFLSRCERFVYYCISVYLFAVVVLCSCWFALDPLFNMWA
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分子量
24.1 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.
Quality inspection process
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Protein Description
The U22 protein, a key component in the study of protein folding and cellular function, has garnered significant attention in recent years due to its role in various biological processes. Originally identified in the context of eukaryotic cells, U22 is implicated in stress response, cellular signaling, and the maintenance of protein homeostasis. The reconstitution and characterization of U22 as a recombinant protein represent a crucial step in understanding its structure-function relationship. Utilizing techniques such as molecular cloning, expression in heterologous systems, and purification protocols, researchers aim to elucidate the protein's stability, interaction dynamics, and functional mechanisms. This research is particularly relevant given that misfolded proteins are associated with various diseases, including neurodegenerative disorders. Thus, studying U22 not only enhances our fundamental knowledge of protein biology but also opens avenues for potential therapeutic applications, ultimately contributing to advancements in biomolecular engineering and medicine.
