Analytical Data
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基因名
DEFa2
- Application
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别名
Defcr2; Defensin-Related Cryptdin-2; Cryptdin-1
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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 & GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P59665
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表达区间
Gln18~Cys94
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分子量
38kDa
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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
DEFa2, also known as Defensin alpha 2, is a member of the defensin family of antimicrobial peptides that play a crucial role in the innate immune response. The study of DEFa2 and its recombinant form has garnered significant attention due to its potential applications in therapeutic interventions and its role in host defense mechanisms. Research indicates that DEFa2 displays antimicrobial properties against a wide range of pathogens, including bacteria, viruses, and fungi, making it a promising candidate for developing new antimicrobial agents, especially in the context of rising antibiotic resistance. Additionally, DEFa2 is implicated in modulating inflammation and immune responses, further highlighting its significance in various pathological conditions. Recent advancements in recombinant DNA technology have enabled the expression and purification of DEFa2, allowing for detailed studies into its structure-function relationships and therapeutic potential. Understanding the biophysical characteristics and mechanisms of action of DEFa2 could lead to novel strategies for enhancing innate immunity or designing new drugs that mimic its functions. Moreover, as researchers explore its role in specific diseases, including infections and inflammatory disorders, DEFa2's profile as a multifunctional peptide continues to evolve, solidifying its importance in both basic and applied biomedical research.
