Analytical Data
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基因名
DTNa
- Application
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别名
DTN-A; DRP3; DTN; LVNC1; Dystrophin-Related Protein 3
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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
Q9Y4J8
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表达区间
Met1~Glu288
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分子量
36kDa
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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
DTNa, a recombinant protein derived from the tetanus toxin, has garnered significant attention in scientific research due to its potential applications in various fields, including vaccine development and neurobiology. The understanding of the structure and function of DTNa is crucial because it serves as a key component in the design of improved vaccines against tetanus. The protein’s ability to act as a non-toxic carrier for antigen delivery makes it a valuable tool for generating immune responses without the risks associated with the entire toxin. Furthermore, DTNa's unique interactions with neuronal cells have opened new avenues in the study of synaptic transmission and neurodegenerative diseases. Research has focused on the optimization of DTNa production through recombinant techniques, allowing for higher yields and better functional properties. Additionally, the exploration of DTNa's immunogenicity, stability, and pharmacokinetics is vital for advancing its use in clinical settings. Overall, the investigation of DTNa as a recombinant protein not only enhances our understanding of its biological mechanisms but also paves the way for innovative therapeutic strategies against diseases associated with the tetanus toxin and related neurological disorders.
