Analytical Data
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Gene name
dnaB
- Application
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Alternative Names
dnaB; c5026Replicative DNA helicase; EC 3.6.4.12
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Species
Escherichia coli O6:H1
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8FB22
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Expression Region
1-471aa
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Molecular Weight
58.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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.
