Analytical Data
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基因名
Ecel1
- Application
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别名
Damage-induced neuronal endopeptidase Xce protein Dine, Xce
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种属
Mouse
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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
Q9JMI0
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表达区间
1-61aa
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分子量
13.7 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
Ecel1, a member of the E-Cell family, is a novel recombinant protein that has garnered attention in recent years due to its potential applications in biotechnology and medicine. Research into Ecel1 emerged from the growing demand for proteins that can serve specific functions in various biological processes, including cell signaling, immune response, and tissue repair. Its unique structural properties and biological activities suggest that Ecel1 may play a significant role in modulating cellular functions and could be a valuable tool in therapeutic interventions. Initial studies have focused on the protein's expression, purification, and characterization, revealing its stability and activity under physiological conditions. Furthermore, investigations into its interactions with other biomolecules have provided insights into its functional mechanisms. As the landscape of protein engineering continues to evolve, understanding the intricacies of Ecel1’s functionality will be crucial for developing innovative strategies for drug design, regenerative medicine, and other applications in life sciences. Continued research on Ecel1 will likely unlock new opportunities for harnessing its properties in scientific and clinical settings. The increasing interest from the scientific community highlights the importance of Ecel1 as a model for studying protein function and its potential to address pressing challenges in health and disease.
