Analytical Data
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基因名
hmfB
- Application
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别名
hmfB；DNA-binding Protein HMf-2
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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
P19267
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表达区间
1-69aa
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氨基酸序列
MELPIAPIGRIIKDAGAERVSDDARITLAKILEEMGRDIASEAIKLARHAGRKTIKAEDIELAVRRFKK
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分子量
9.7 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
Research on HmfB recombinant protein has gained significant attention due to its potential applications in biotechnology and medicine. HmfB, a protein derived from certain microorganisms, is known for its ability to bind and transport metal ions, playing a crucial role in microbial metalloproteomics. Its unique structure and binding properties make it a candidate for various applications, including bioremediation, biosensors, and as a therapeutic agent in metal ion-related diseases. The recombinant expression of HmfB allows for large-scale production and detailed study of its functional properties, enabling scientists to explore its interactions with different metal ions and its potential role in cellular processes. Furthermore, the engineering of HmfB for enhanced stability and specificity can lead to breakthroughs in developing environmentally friendly technologies. Understanding the underlying mechanisms of HmfB function also contributes to the broader field of metalloprotein research, which is essential for advancing knowledge on metal homeostasis in biological systems. Overall, the exploration of HmfB recombinant protein holds promise for innovative solutions in environmental science and health-related applications.
