Analytical Data
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基因名
DEFb103A
- Application
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别名
DEFb103A；BD3；DEFB103；DEFB3；Beta-defensin 103
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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
P81534
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表达区间
23-67aa
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氨基酸序列
GIINTLQKYYCRVRGGRCAVLSCLPKEEQI GKCSTRGRKCCRRKK
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分子量
5 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 study of the recombinant protein DEFb103A, a member of the defensin family, is rooted in its potential role as an innate immune effector. Defensins are small, cationic peptides that possess broad-spectrum antimicrobial properties, playing a crucial role in the defense against pathogens. They are produced by various organisms, including plants, insects, and mammals, highlighting their evolutionary significance in immune responses. DEFb103A, specifically identified in certain amphibian species, has garnered attention due to its unique structural attributes and effective antimicrobial activity against bacteria and fungi. Research has suggested that this protein not only serves as a defensive barrier but may also participate in wound healing and modulating inflammation. Understanding the mechanism of action and structure-function relationships of DEFb103A could pave the way for developing new therapeutic agents or enhancing existing antimicrobial strategies. As resistance to conventional antibiotics rises, exploring natural antimicrobial peptides like DEFb103A presents a promising avenue for drug discovery and development, emphasizing the importance of investigating this protein within the broader context of antimicrobial research and immunology.
