Analytical Data
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Gene name
OAZ3
- Application
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A1BPI0
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Expression Region
Leu1~Ser86
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Molecular Weight
14kDa
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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
OAZ3, or Ornithine Decarboxylase Antizyme 3, is a key regulatory protein involved in polyamine metabolism, which plays a crucial role in cell growth, differentiation, and apoptosis. The study of OAZ3 has gained significance due to its potential implications in various biological processes and diseases, including cancer, where dysregulation of polyamine levels can lead to uncontrolled cell proliferation. OAZ3, as part of the antizyme family, is known to inhibit ornithine decarboxylase (ODC), the enzyme responsible for the first step in polyamine synthesis. Understanding the structure and function of OAZ3 can provide valuable insights into its regulatory mechanisms and how it interacts with other cellular components. Recent research has highlighted the importance of OAZ3 in modulating polyamine levels and its involvement in atypical cellular responses to stress and environmental changes. By exploring the role of OAZ3 at the molecular level, researchers hope to uncover new therapeutic targets for diseases associated with altered polyamine metabolism, thereby contributing to the development of novel treatment strategies. The ongoing investigation into the OAZ3 protein not only enhances our understanding of cellular growth regulation but also expands the potential for clinical applications in the management of polyamine-related disorders.
