Analytical Data
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Gene name
RuvC
- Application
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Alternative Names
Holliday junction nuclease RuvCHolliday junction resolvase RuvC
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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
P0A814
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Expression Region
2-173aa
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Molecular Weight
34.6 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
RuvC is a crucial recombinase enzyme that plays a significant role in DNA repair and homologous recombination, essential processes for maintaining genomic stability in cells. It is a part of the RuvC family of proteins, which are involved in resolving Holliday junctions, intermediates formed during homologous recombination. These junctions can arise during DNA replication or repair, and their proper resolution is vital to prevent genetic instability and ensure accurate DNA inheritance. Research on RuvC has gained momentum due to its implications in understanding various biological processes, including cellular responses to DNA damage, bacterial resistance to antibiotics, and the mechanisms underpinning certain genetic disorders. Studying RuvC not only enhances our comprehension of DNA repair pathways but also provides insights into potential therapeutic targets for diseases stemming from genomic instability, such as cancer. Advances in structural biology, including X-ray crystallography and cryo-electron microscopy, have shed light on the molecular mechanisms of RuvC function, revealing how it interacts with DNA substrates and other proteins involved in recombination. The ongoing exploration of RuvC's roles in different organisms, including bacteria and eukaryotes, underscores its evolutionary significance and broad relevance in biological research.
