Analytical Data
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基因名
sbi
- Application
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别名
sbi;CPAMD1;Complement C3
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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
Q2FVK5
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表达区间
30-436aa
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氨基酸序列
SENTQQTSTKHQTTQNNYVTDQQKAFYQVLHLKGITEEQRNQYIKTLREHPERAQEVFSESLKDSKNPDRRVAQQNAFYNVLKNDNLTEQEKNNYIAQIKENPDRSQQVWVESVQSSKAKERQNIENADKAIKDFQDNKAPHDKSAAYEANSKLPKDLRDKNNRFVEKVSIEKAIVRHDERVKSANDAISKLNEKDSIENRRLAQREVNKAPMDVKEHLQKQLDALVAQKDAEKKVAPKVEAPQIQSPQIEKPKVESPKVEVPQIQSPKVEVPQSKLLGYYQSLKDSFNYGYKYLTDTYKSYKEKYDTAKYYYNTYYKYKGAIDQTVLTVLGSGSKSYIQPLKVDDKNGYLAKSYAQVRNYVTESINTGKVLYTFYQNPTLVKTAIKAQETASSIKNTLSNLLSFWK
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分子量
54.0 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
SBI (Siderocalin Binding Protein) is a protein that has garnered significant interest in the field of biochemistry and molecular biology due to its role in iron homeostasis and host-pathogen interactions. The research surrounding SBI has primarily focused on its ability to sequester iron, an essential element for bacterial survival, thus acting as a critical component of the innate immune response. During infectious processes, pathogens often exploit iron to proliferate, making SBI a potential target for therapeutic interventions. Studies have shown that SBI binds to siderophores, which are molecules produced by bacteria to capture iron from the host. This binding not only reduces the availability of iron but also modulates the inflammatory response, impacting the outcome of infections. Furthermore, the understanding of SBI's structure and function can provide insights into novel drug design, particularly in the development of agents that can disrupt pathogenic iron acquisition. Research in this area is also expanding to include the exploration of SBI’s interaction with various pathogens, thereby elucidating its potential role in diverse diseases, including tuberculosis and other iron-related disorders. The ongoing investigations into SBI's mechanisms may pave the way for innovative approaches in the treatment of infections, highlighting its significance in both fundamental biological research and clinical applications. Overall, the study of SBI and its functional properties holds promise for advancing our knowledge of immune mechanisms and developing new strategies to combat infectious diseases.












