Analytical Data
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基因名
AaH
- Application
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别名
AaH II Short name:AaHII Neurotoxin 2
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种属
Androctonus australis
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P01484
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表达区间
20-83aa
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分子量
23.3 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
Related Products
Protein Description
The study of AaH recombinant protein is rooted in the need to understand the biological properties and potential applications of proteins derived from the venom of the Androctonus australis hector scorpion. Research on scorpion venom has gained significant attention due to its diverse pharmacological effects and the unique bioactive components it contains, including proteins, peptides, and enzymes. AaH, a major component of this venom, is known for its neurotoxic effects, which can lead to various physiological responses in prey and can have implications for human health. By producing AaH as a recombinant protein, scientists aim to overcome challenges related to its extraction and purification from natural sources, enabling detailed studies of its structure, function, and potential therapeutic uses. Additionally, recombinant technology facilitates the modification of the protein to enhance its properties or reduce its toxicity, paving the way for novel biomedical applications, such as analgesics, treatments for autoimmune diseases, or as tools in molecular biology. As such, the investigation of AaH recombinant protein holds promise for advancing both basic research in toxinology and practical applications in medicine and pharmacology.
