Analytical Data
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Gene name
PRDX6
- Application
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Alternative Names
PRDX6；AOP2；KIAA0106；Peroxiredoxin-6
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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
P30041
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Expression Region
2-224aa
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AA Sequence
PGGLLLGDV APNFEANTTV GRIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE FAKRNVKLIA LSIDSVEDHL AWSKDINAYN CEEPTEKLPF PIIDDRNREL AILLGMLDPA EKDEKGMPVT ARVVFVFGPD KKLKLSILYP ATTGRNFDEI LRVVISLQLT AEKRVATPVD WKDGDSVMVL PTIPEEEAKK LFPKGVFTKE LPSGKKYLRY TPQP
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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
Peroxiredoxin 6 (PRDX6) is a crucial antioxidant enzyme that plays a significant role in cellular defense against oxidative stress and inflammation. It is a member of the peroxiredoxin family, characterized by its ability to reduce hydrogen peroxide and other reactive oxygen species, thus maintaining redox homeostasis within cells. Recent studies have highlighted the multifunctional nature of PRDX6, which not only acts as a peroxidase but also exhibits lysophospholipase activity, contributing to the metabolism of lysophospholipids and the regulation of cell signaling pathways. The dysregulation of PRDX6 expression has been implicated in various pathological conditions, including cancer, neurodegenerative diseases, and cardiovascular disorders. This has spurred interest in the therapeutic potential of PRDX6 as a biomarker and a target for intervention. Recombinant PRDX6 proteins have emerged as valuable tools for elucidating its biological functions and mechanisms of action. They can be utilized to study the enzyme's role in cellular processes, screen for potential inhibitors, and evaluate its impact on disease models. The development of PRDX6 recombinants facilitates a deeper understanding of its structure-function relationship and paves the way for innovative therapeutic strategies aimed at harnessing its antioxidant properties in disease treatment and prevention. This ongoing research underscores the importance of PRDX6 in human health and disease, making it a focal point for future investigations in both basic and translational science.
