Analytical Data
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基因名
HSP100
- Application
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别名
Protein CLP
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种属
Trypanosoma cruzi
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O15885
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表达区间
1-138aa
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分子量
22.9 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
HSP100 proteins are a class of heat shock proteins that play a crucial role in protein quality control, specifically by assisting in the refolding or degradation of misfolded proteins. They are part of the cellular stress response, helping organisms survive under conditions such as heat shock, oxidative stress, and other adverse environmental factors. Research has highlighted their involvement in various cellular processes, such as protein disaggregation, which is vital for maintaining cellular homeostasis. HSP100 proteins have garnered attention in the fields of molecular biology and biomedical research due to their potential therapeutic implications. For instance, their chaperone activity has been studied in the context of neurodegenerative diseases, where the accumulation of misfolded proteins is a hallmark. Recent studies have also explored the recombinant expression of HSP100 proteins, aiming to harness their unique properties for applications in protein engineering, biotechnology, and as therapeutic agents. Understanding the mechanisms by which HSP100 proteins operate can offer insights into their roles in stress responses and their potential use in treating diseases associated with protein misfolding. Thus, ongoing research into HSP100 recombinant proteins holds promise for both fundamental biology and potential medical advancements.
