Analytical Data
-
Gene name
Peroxiredoxin 5
- Application
-
Alternative Names
PRDX3;AOP1;Thioredoxin-dependent peroxide reductase. mitochondrial
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P30044
-
Expression Region
53-214aa
-
AA Sequence
MAPIKVGD AIPAVEVFEG EPGNKVNLAE LFKGKKGVLF GVPGAFTPGC SKTHLPGFVE QAEALKAKGV QVVACLSVND AFVTGEWGRA HKAEGKVRLL ADPTGAFGKE TDLLLDDSLV SIFGNRRLKR FSMVVQDGIV KALNVEPDGT GLTCSLAPNI ISQL
-
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
Peroxiredoxin 5 (Prdx5) is a member of the peroxiredoxin family, a group of antioxidant enzymes that play crucial roles in cellular redox regulation and defense against oxidative stress. This enzyme is notable for its ability to reduce peroxides, thus protecting cells from damage caused by reactive oxygen species (ROS). Research on Prdx5 has gained momentum due to its involvement in various biological processes, including cell signaling, proliferation, and apoptosis. Additionally, it has been linked to several diseases, such as cancer and neurodegenerative disorders, highlighting its potential as a therapeutic target. The recombinant expression of Prdx5 in a laboratory setting enables detailed functional studies, allowing researchers to investigate its enzymatic activity, structure, and interaction with other cellular molecules. By producing recombinant Prdx5, scientists can assess its role in oxidant defense, characterize mutations that may impair its function, and explore its potential as a biomarker for disease states. Overall, the study of recombinant Prdx5 is significant in understanding the enzyme's biological functions and its implications in human health and disease.
