Analytical Data
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Gene name
WRN
- Application
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Alternative Names
WRN；RECQ3；RECQL2；Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q14191
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Expression Region
500-946aa
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AA Sequence
NLGLPTKEEEEDDENEANEGEEDDDKDFLWPAPNEEQVTCLKMYFGHSSFKPVQWKVIHSVLEERRDNVAVMATGYGKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQSENVLTDIKLGKYRIVYVTPEYCSGNMGLLQQLEADIGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGFDRPNLYLEVRRKTGNILQDLQPFLVKTSSHWEFEGPTIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTEIRNEKFRLYKLKMMAKMEKYLHSSRCRRQIILSHFEDKQVQKASLGIMGTEKCCDNCRSRLDHC
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Molecular Weight
56.8 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
The study of WRN (Werner Syndrome ATP-dependent helicase), a member of the RecQ helicase family, has garnered significant interest due to its role in maintaining genome stability and its implications in aging and cancer. WRN is characterized by its involvement in DNA repair processes, where it unwinds DNA structures and plays a critical role in replication fork maintenance and the repair of double-strand breaks. Mutations in the WRN gene lead to Werner syndrome, a premature aging disorder marked by features such as sarcomas, atherosclerosis, and other age-related diseases. Understanding the biochemical properties and functions of WRN is essential, as it not only provides insights into the mechanisms of cellular aging but also highlights potential therapeutic targets for age-associated pathologies and tumorigenesis. The exploration of WRN as a recombinant protein further facilitates the study of its enzymatic activities, interactions with other proteins involved in DNA repair, and the development of compounds that may enhance or inhibit its function, thereby contributing to the field of molecular biology and potential clinical applications. The ongoing research aims to elucidate the detailed mechanisms of WRN action and its broader implications in human health, emphasizing the need for comprehensive studies into its structure and functional properties.
