Analytical Data
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Gene name
RuvA
- Application
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Alternative Names
ruvA; b1861; JW1850; Holliday junction ATP-dependent DNA helicase RuvA; EC 3.6.4.12
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0A809
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Expression Region
1-203aa
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Molecular Weight
38.1 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
RuvA is a crucial protein involved in the bacterial DNA repair process, particularly in the resolution of DNA recombination intermediates during homologous recombination. This protein plays a key role in maintaining genomic stability by helping to process Holliday junctions, which are formed during the exchange of genetic material between homologous DNA strands. Understanding the structure and function of RuvA is vital as it not only provides insights into fundamental biological processes but also has implications for therapeutic developments, particularly in combating antibiotic resistance. Research into RuvA has demonstrated that it operates as a part of a larger protein complex, often in conjunction with RuvB and RuvC, to effectively manage DNA repair. Mutations or malfunctions in this system can lead to a variety of complications, including increased susceptibility to DNA-damaging agents and impaired cellular repair mechanisms. As such, studying RuvA and its interactions with other proteins can reveal potential targets for novel antibiotics and contribute to our understanding of DNA repair pathways in bacteria, ultimately enhancing efforts to develop strategies against bacterial infections. Additionally, RuvA’s mechanisms may provide parallels in eukaryotic systems, thereby enriching the broader field of molecular biology and genetics. Overall, RuvA research not only enhances our comprehension of bacterial DNA repair but also opens avenues for innovative clinical applications.
