Analytical Data
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Gene name
SRXN1
- Application
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Alternative Names
SRXN1；C20orf139；SRX；SRX1；Sulfiredoxin-1
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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
Q9BYN0
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Expression Region
1-137aa
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AA Sequence
MGLRAGGTLGRAGAGRGAPEGPGPSGGAQGGSIHSGRIAAVHNVPLSVLIRPLPSVLDPAKVQSLVDTIREDPDSVPPIDVLWIKGAQGGDYFYSFGGCHRYAAYQQLQRETIPAKLVQS
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Molecular Weight
19.9 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
Related Products
Protein Description
SRXN1 (sulfiredoxin 1) is a pivotal antioxidant enzyme that plays a crucial role in cellular defense mechanisms against oxidative stress. It is primarily known for its ability to reduce hyperoxidized peroxiredoxins, thus maintaining redox homeostasis within the cell. The regulation of oxidative stress is vital for various physiological processes, including cell signaling, apoptosis, and inflammation. Dysregulation of SRXN1 expression has been implicated in several diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases, highlighting its potential as a therapeutic target. Furthermore, SRXN1 is involved in various stress response pathways, working alongside other antioxidant proteins to protect cells from damage caused by reactive oxygen species (ROS). Understanding the structure and function of SRXN1, including the characterization of its recombinant protein, is essential for elucidating its biological role and therapeutic potential. Researchers are increasingly focused on the recombinant production of SRXN1 to explore its enzymatic activity, protein interactions, and post-translational modifications. This research aims to provide insights into the functional biology of SRXN1, enabling the development of targeted therapies that exploit its antioxidant properties to counteract oxidative damage in various diseases. By investigating the recombinant expression and activity of SRXN1, scientists hope to uncover novel strategies for enhancing cellular resilience against oxidative stress and promoting tissue repair and regeneration, thereby contributing to advances in disease management and therapeutic interventions.
