Analytical Data
-
Gene name
WRN
- Application
-
Alternative Names
(DNA helicase, RecQ-like type 3)(RecQ3)(Exonuclease WRN)(RecQ protein-like 2)
-
Species
Human
-
Source
E. coli
-
Tag
N- MBP & C- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q14191
-
Expression Region
500-946aa
-
Molecular Weight
94.6 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
The study of WRN (Werner Syndrome RecQ Helicase) protein is deeply rooted in its significance in human health and disease. WRN is a member of the RecQ helicase family, crucial for maintaining genomic stability and facilitating DNA repair, replication, and recombination processes. Mutations in the WRN gene lead to Werner syndrome, a rare progeroid disorder characterized by premature aging and increased susceptibility to age-related diseases such as cancer, diabetes, and cardiovascular issues. Research into the WRN protein has expanded due to its critical role in various cellular processes essential for preventing genomic instability, which is a hallmark of cancer progression. Investigating WRN's structure and function can provide insights into its helicase activity and interactions with other proteins involved in DNA metabolism. Furthermore, understanding WRN's cellular mechanisms may unveil potential therapeutic targets for alleviating the effects of Werner syndrome and related disorders, emphasizing the importance of WRN research in the broader context of aging and cancer biology. Through advanced techniques such as X-ray crystallography and cryo-electron microscopy, researchers aim to elucidate the intricacies of WRN's function, paving the way for innovative treatments and preventive strategies against the ailments associated with its dysfunction.
