Analytical Data
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基因名
DERP5
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简介
DERP5 protein exhibits a monomeric structure and forms homodimeric trimers through concentration-dependent oligomerization, which plays a key role in allergic reactions. Multiple population studies have shown that DERP5 binds to IgE and is associated with mite allergy symptoms such as asthma and rhinitis. DERP5 Protein, Dermatophagoides pteronyssinus (His) is the recombinant DERP5 protein, expressed by E. coli , with N-His labeled tag.
- Application
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别名
Mite allergen Der p 5; Allergen Der p V; IgE-binding allergen; Der p 5
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种属
Others
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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
P14004
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表达区间
M1-V132
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蛋白长度
Full Length
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分子量
15 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
DERP5, or Defensin-related protein 5, is a member of the defensin family known for its antimicrobial properties, predominantly expressed in the respiratory and reproductive tissues of various species. Its role has garnered significant interest due to its potential involvement in innate immunity, where it might contribute to the host defense against pathogens. Studies have indicated that DERP5 exhibits unique structural features that may enhance its functional attributes, prompting researchers to investigate its biophysical properties and possible therapeutic applications. Understanding the expression regulation of DERP5 in response to infections or inflammatory stimuli is crucial, as it could lead to new insights into disease mechanisms and the development of novel interventions. Additionally, the recombinant production of DERP5 facilitates detailed studies on its structure-function relationship, enabling exploration of its potential as a biomarker or a therapeutic agent in enhancing immune responses. As research progresses, DERP5 may play a pivotal role in advancing our knowledge of antimicrobial peptides and their applications in medical science.
