Analytical Data
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基因名
tbpA
- Application
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别名
(TbpA)(Transferrin-binding protein 1)
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种属
Haemophilus influenzae
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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
P44970
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表达区间
24-912aa
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分子量
102.9 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 research on the tbpA recombinant protein is rooted in the need for understanding the TbpA protein's role in the pathogenesis of pathogenic bacteria, particularly in relation to human infections. TbpA, or transferrin-binding protein A, is crucial for iron acquisition, a vital process for bacterial survival and virulence. Many pathogens, such as Neisseria meningitidis and Haemophilus influenzae, rely on TbpA to capture iron from the host's transferrin, thereby facilitating their growth and infection. The study of tbpA has significant implications for developing novel therapeutic strategies, as targeting this protein could potentially disrupt iron acquisition and limit bacterial proliferation. Furthermore, recombinant forms of TbpA can be synthesized for use in vaccine development, aiming to elicit an immune response that can protect against these infections. Advancements in recombinant DNA technology have enabled researchers to produce large quantities of tbpA, allowing for detailed investigations into its structure, function, and interaction with host immune components. Understanding the mechanisms by which tbpA operates not only elucidates the fundamental biology of pathogenic bacteria but also holds promise for innovative approaches to combat bacterial infections, ultimately contributing to improved human health outcomes.












