Analytical Data
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Gene name
uvrD
- Application
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Alternative Names
mutU, pdeB, rad, recL
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Species
Escherichia coli
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P03018
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Expression Region
1-720aa
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Molecular Weight
82 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
UvrD, also known as helicase II or UvrD helicase, is a crucial protein involved in DNA repair and maintenance in various organisms. It plays a significant role in the nucleotide excision repair (NER) pathway, which is essential for repairing bulky DNA lesions caused by environmental factors, such as UV radiation and chemical exposure. The importance of UvrD is underscored by its involvement in other cellular processes, including DNA replication and the progression of RNA transcription. Researchers focus on the recombination of UvrD to understand its structural and functional dynamics, which can reveal insights into its mechanism of action as a helicase. Exploring the biochemical properties of UvrD recombinants can help elucidate the underlying processes of DNA repair and may identify potential therapeutic targets for diseases linked to DNA damage, including cancer. Additionally, studying UvrD can enhance our understanding of the evolution of DNA repair systems across different species, providing a comparative framework for analyzing the effectiveness of these mechanisms in various cellular environments. As such, the recombinant study of UvrD protein represents a critical area of inquiry in molecular biology and genetic research, with implications for biotechnology and medicine.
