Analytical Data
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Gene name
PXDN
- Application
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Alternative Names
PXDN；KIAA0230；MG50；PRG2；Peroxidasin homolog
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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
Q92626
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Expression Region
1452-1561aa
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AA Sequence
STSAFSTRSDASGTNDFREFVLEMQKTITDLRTQIKKLESRLSTTECVDA GGESHANNTKWKKDACTICECKDGQVTCFVEACPPATCAVPVNIPGACCP VCLQKRAEEK
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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
PXDN (Peroxidase Domain Containing Protein) is a member of the peroxidase enzyme family, which plays a crucial role in various biological processes, including the regulation of reactive oxygen species (ROS), cellular signaling, and immune responses. Recent studies have highlighted its potential involvement in inflammatory conditions and tumor biology, suggesting that PXDN may be a critical mediator in the oxidative stress response of cells. Given its diverse physiological roles, researchers have focused on understanding the structural and functional characteristics of PXDN, particularly through recombinant protein studies. The expression and purification of PXDN as a recombinant protein facilitate the investigation of its enzymatic activities, substrate specificity, and biological interactions. These studies are essential for elucidating the molecular mechanisms of PXDN in health and disease, ultimately paving the way for potential therapeutic applications targeting oxidative stress-related conditions. Moreover, as PXDN's role in the formation of extracellular matrix components and its implication in fibrosis have been recognized, researchers are actively exploring its potential as a biomarker and therapeutic target in fibrotic diseases. As such, the study of PXDN recombinant protein has become a significant area of interest, providing insights not only into fundamental biological processes but also into the development of novel strategies for the treatment of various diseases associated with oxidative stress and inflammation.
