Analytical Data
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基因名
dnaB
- Application
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别名
dnaB; c5026Replicative DNA helicase; EC 3.6.4.12
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种属
Escherichia coli O6:H1
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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
Q8FB22
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表达区间
1-471aa
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分子量
58.4 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 DNA B helicase (dnaB) has garnered significant attention due to its crucial role in bacterial DNA replication and cell cycle regulation. DnaB is a hexameric helicase predominantly found in Escherichia coli and other Gram-negative bacteria, functioning to unwind double-stranded DNA ahead of the replication fork. This activity is essential for the proper progression of DNA replication, as it allows for the synthesis of the leading and lagging strands. The complexity of the DNA replication machinery, in which DnaB operates alongside other key proteins, makes it a vital subject for understanding the mechanisms of bacterial growth and division. In recent years, research has shifted towards elucidating the structural and functional dynamics of DnaB, revealing insights into its interaction with primase, single-stranded binding proteins, and other replication factors. Moreover, DnaB's integral role in DNA repair and its potential as a target for antibiotic development highlight the importance of these studies in both microbiology and pharmaceutical research. Understanding the molecular mechanisms by which DnaB operates can provide foundational knowledge for innovations in treating bacterial infections and combating antibiotic resistance. As such, ongoing research into DnaB's biochemical properties, regulation, and interaction networks continues to be a thriving area of investigation with implications for both fundamental biology and applied sciences.
