Analytical Data
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Gene name
recQ
- Application
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Alternative Names
recQ; b3822; JW5855; ATP-dependent DNA helicase RecQ; 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
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P15043
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Expression Region
2-606aa
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Molecular Weight
71.9 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
Related Products
Protein Description
RecQ helicases are a family of enzymes that play critical roles in maintaining genomic stability by unwinding DNA during processes such as replication, repair, and recombination. Mutations in RecQ helicases are associated with several human disorders, including Werner Syndrome, Bloom Syndrome, and Rothmund-Thomson Syndrome, which are characterized by increased cancer susceptibility and premature aging. The functional importance of RecQ proteins lies in their ability to resolve DNA structures that can potentially lead to genomic instability, such as secondary structures formed during DNA replication or repair. Research on recombinant RecQ proteins has advanced our understanding of their biochemical activities, regulatory mechanisms, and interactions with other proteins involved in DNA metabolism. Utilizing recombinant techniques allows for the production of these helicases in large quantities, facilitating detailed studies of their enzymatic properties, substrate specificity, and the molecular basis of their roles in DNA maintenance pathways. Furthermore, exploring these proteins in the context of their involvement in various DNA repair mechanisms has provided insights into potential therapeutic targets for cancer treatment and aging-related diseases. Understanding the structure-function relationships of RecQ helicases can shed light on their precise roles in cellular processes and their implications for human health. Overall, the study of recombinant RecQ proteins is essential for elucidating the complexities of genomic stability and the molecular underpinnings of diseases linked to helicase deficiencies.
