Analytical Data
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基因名
inaX
- Application
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别名
/
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种属
Xanthomonas campestris pv. translucens
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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
P18127
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表达区间
1412-1567aa
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分子量
22.3 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 recombinant proteins, particularly in the context of insulin-like growth factor (IGF) and its analogs, has garnered significant attention in the field of molecular biology and biotechnology. One notable product is the inaX recombinant protein, which is engineered to enhance therapeutic benefits while minimizing side effects associated with traditional treatments. Advances in genetic engineering have allowed scientists to manipulate the DNA sequences encoding these proteins, leading to increased expression levels and improved functionality. Research has shown that inaX may play a pivotal role in biological processes such as cell growth, differentiation, and metabolism. The recombinant production methods enable large-scale synthesis of inaX, facilitating studies on its mechanism of action and potential applications in regenerative medicine and cancer therapeutics. Moreover, despite the promise shown by recombinant proteins, challenges regarding their stability, scalability, and post-translational modifications remain, necessitating ongoing research. The exploration of inaX and similar proteins not only broadens the understanding of IGF-related pathways but also holds the potential for innovative treatments in various diseases, underscoring the importance of continued investigations in this promising area of biotechnology.
