Analytical Data
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基因名
spi
- Application
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别名
spi; Spiralin
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种属
Spiroplasma citri
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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
P19215
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表达区间
24-241aa
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分子量
39 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
The study of SPI (Serpin Protease Inhibitor) recombinant proteins has gained significant attention in recent years due to their vital role in regulating proteolysis, which is essential for various physiological processes, including the immune response, coagulation, and inflammation. Serpins are a superfamily of proteins that function primarily as inhibitors of serine proteases, and their dysregulation has been implicated in numerous diseases, such as thrombosis, cancer, and neurodegenerative disorders. Given their importance, researchers have increasingly focused on the production of recombinant SPI proteins for therapeutic and diagnostic applications. These recombinantly produced proteins offer advantages over their natural counterparts, including increased purity, enhanced stability, and the ability for site-directed mutagenesis to improve efficacy. Advances in biotechnology have facilitated the development of various expression systems, such as bacterial, yeast, and mammalian cells, to optimize the yield and functionality of SPI proteins. Furthermore, understanding the structure-activity relationship of these inhibitors aids in the design of novel drugs targeting specific proteases involved in disease pathways. Overall, the exploration of SPI recombinant proteins could lead to innovative treatments and advancements in the field of biomedicine, making it a promising area of ongoing research.












