Analytical Data
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基因名
SP-C
- Application
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别名
SP-C;GC1QBP;HABP1;SF2P32;Complement component 1 Q subcomponent-binding Protein. mitochondrial
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P11686
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表达区间
24-58aa
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氨基酸序列
FGIPCCPVHLKRLLIVVVVVVLIVVVIVGALLMGL
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分子量
5.7kDa
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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
Surfactant Protein C (SP-C) is a pivotal component of pulmonary surfactant, crucial for reducing surface tension in the alveoli, thereby preventing lung collapse during exhalation and ensuring efficient gas exchange. The gene encoding SP-C is located on chromosome 8, and mutations or deficiencies in this protein can lead to severe respiratory conditions, such as surfactant dysfunction disorders and interstitial lung disease. The study of SP-C has become increasingly significant, particularly in understanding its role in lung health and disease, as well as in the development of therapeutic interventions. Recombinant SP-C proteins, produced using biotechnological methods, have emerged as potential therapeutic agents in treating surfactant abnormalities. Research has focused on the structure-function relationship of SP-C, exploring how modifications in the protein can enhance its stability and functionality. Furthermore, investigations into the molecular mechanisms by which SP-C interacts with lipids and other proteins in surfactant complexes provide valuable insights into respiratory physiology. Recent advances in gene therapy and protein engineering aim to correct SP-C deficiencies, offering hope for patients suffering from related pulmonary disorders. This underscores the importance of SP-C recombinant protein research in developing novel strategies for the prevention and treatment of various lung diseases.












