Analytical Data
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基因名
isaB
- Application
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别名
isaB;Immunodominant staphylococcal antigen B
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种属
E.coli
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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
Q9LAB5
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表达区间
37-175aa
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氨基酸序列
AITPYYTYNGYIGNNANFILDKNFINAIKYDNVKFNGIKLAKTNTIKKVEKYDQTFKGVSAKGNEASQLQFVVKNNISLKDIQKAYGKDLKKENGKTKEADSGIFYYQNAKKTLGIWFVVDHNRVVEVTVGHTPYKTSK
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分子量
20.8 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 IsaB recombinant protein is rooted in the growing interest in understanding the mechanisms of bacterial pathogenesis and the development of novel therapeutic strategies. IsaB, a protein associated with the pathogenicity of certain bacterial species, plays a crucial role in regulating iron homeostasis and facilitating the uptake of iron, an essential nutrient for bacterial survival and growth. The lack of effective treatments against antibiotic-resistant bacteria has heightened the urgency for new approaches, including the exploration of protein-based therapies. Research on IsaB is particularly significant due to its potential as a target for drug design, as inhibiting its function may disrupt bacterial iron acquisition, thereby attenuating virulence. Advances in recombinant DNA technology have enabled the production of IsaB in heterologous expression systems, allowing for detailed structural and functional studies. Understanding the three-dimensional structure of IsaB through techniques such as X-ray crystallography and cryo-electron microscopy can provide insights into its interaction with host factors and reveal potential binding sites for therapeutic agents. Furthermore, the characterization of IsaB's immunogenic properties may lead to the development of vaccine candidates against pathogenic bacteria. Overall, the exploration of IsaB recombinant protein is a vital endeavor in the field of microbiology, with implications for vaccine development, therapeutic interventions, and the mitigation of infectious diseases.












