Analytical Data
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基因名
isdA
- Application
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别名
Fur-regulated protein A Staphylococcal transferrin-binding protein A frpA, stbA
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种属
Staphylococcus aureus
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q6GA85
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表达区间
47-316aa
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分子量
35.1 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
IsdA (Iron-regulated surface determinant A) is a significant component in the pathogenicity of certain bacterial strains, particularly Staphylococcus aureus. Understanding the structure and function of IsdA is crucial as it plays a pivotal role in iron acquisition, which is vital for bacterial survival and proliferation in the iron-limited environments of a host organism. Research has shown that IsdA interacts with hemoglobin, facilitating the extraction of heme, an iron-containing compound that bacteria utilize for their metabolic processes. This mechanism underscores the importance of IsdA not only in the context of bacterial virulence but also as a potential target for novel therapeutic strategies aimed at combatting infections. The study of IsdA is further accentuated by the increasing prevalence of antibiotic-resistant strains of S. aureus, prompting the need for alternative approaches to treatment. Recombinant IsdA proteins have been generated for detailed structural studies and functional assays, allowing researchers to explore the molecular mechanisms underlying heme uptake. These studies offer insights into the interaction of IsdA with host proteins and the potential for developing vaccines or inhibitors based on its structure. As such, ongoing research into IsdA and its recombinant forms represents a vital intersection of microbiology, biochemistry, and medical research, promising to advance our understanding of bacterial pathogenesis and lead to innovative solutions in infectious disease management.












