Analytical Data
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基因名
DEFb112
- Application
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别名
DEFB-12
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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 90% as determined by SDS-PAGE.
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蛋白编号
Q30KQ8
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表达区间
Met1~His113
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分子量
17kDa
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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 research on the recombinant protein DEFb112 has gained significant attention due to its potential applications in various fields, including immunology, biotechnology, and medicine. DEFb112 is a member of the defensin family, which comprises antimicrobial peptides that play a crucial role in the innate immune response of organisms. These peptides are known for their ability to combat a wide range of pathogens, including bacteria, fungi, and viruses, making them valuable for therapeutic use. The structural and functional characteristics of DEFb112 have been studied to understand its mechanism of action and potential as an antimicrobial agent. Advances in recombinant DNA technology have enabled the efficient production of DEFb112, facilitating in-depth studies of its biological properties and interactions with microbial targets. Additionally, the ability to modify and optimize the protein for enhanced stability and efficacy has opened avenues for developing novel therapeutic strategies. Researchers are particularly interested in DEFb112's role in boosting immune responses and its potential application in treating infectious diseases, bolstering immunotherapies, and developing new antibiotic alternatives amid rising antibiotic resistance. Overall, the ongoing research on DEFb112 represents a promising direction in the fight against infectious diseases and highlights the importance of antimicrobial peptides in modern medicine.
