Analytical Data
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基因名
DERF3
- Application
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别名
(Allergen Der f III)(allergen Der f 3)
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种属
Dermatophagoides farinae
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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 90% as determined by SDS-PAGE.
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蛋白编号
P49275
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表达区间
28-259aa
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分子量
29.0 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
DERF3 is a recombinant protein that has garnered increasing attention in recent years due to its potential applications in various fields such as immunology, biotechnology, and medicine. Originally identified from certain plant and microbial sources, DERF3 is known for its role in stress response and defense mechanisms. Researchers have been investigating its structure and function to understand how it interacts with biological systems. The protein exhibits unique properties, including stability under extreme conditions and the ability to evoke significant immunogenic responses, making it a promising candidate for vaccine development. Additionally, studies suggest that DERF3 could play a critical role in enhancing plant resistance to pathogens, thus holding promise for agricultural applications. As recombinant DNA technology has advanced, scientists have aimed to produce DERF3 in greater quantities and purities, which has facilitated in-depth functional studies and the potential development of DERF3-based therapeutics. Given the global challenges posed by infectious diseases and food security, the ongoing research into DERF3 recombinant protein is vital for unlocking its full potential and translating these findings into practical solutions.
