Analytical Data
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Gene name
RuvB
- Application
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Alternative Names
ruvB; b1860; JW1849; Holliday junction ATP-dependent DNA helicase RuvB; 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
P0A812
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Expression Region
1-336aa
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Molecular Weight
53.2 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
RuvB helicases are a family of proteins that play a crucial role in the repair and maintenance of DNA, particularly during the processes of homologous recombination and DNA replication. These proteins are characterized by their ATP-dependent helicase activity, which allows them to unwind double-stranded DNA, facilitating various DNA repair mechanisms. The significance of RuvB proteins is particularly highlighted in bacteria, where they assist in the resolution of Holliday junctions—intermediates formed during homologous recombination. Their proper function is essential for maintaining genomic stability and preventing mutations that could lead to diseases, including cancer. Research on RuvB proteins has also expanded to eukaryotic systems, where similar helicase activities have been implicated in critical cellular processes. Understanding the structure and function of RuvB proteins not only provides insight into fundamental biological processes but also poses potential therapeutic implications. Targeting these proteins could lead to novel strategies in cancer treatment and strategies against antibiotic-resistant bacterial infections, making them a focal point in both molecular biology and medical research. Recent advances in structural biology techniques, such as X-ray crystallography and cryo-electron microscopy, have enhanced our comprehension of RuvB protein mechanisms, revealing intricate details of their action at the molecular level. Additionally, studies are increasingly examining the regulatory pathways controlling RuvB expression and activity, emphasizing its relevance in the broader context of cellular stress responses and DNA damage repair networks. Consequently, RuvB helicases are not only vital for their biological functions but also serve as valuable models for exploring the complexities of DNA dynamics in living organisms.
