Analytical Data
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Gene name
OAZ1
- Application
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Alternative Names
AZI; OAZ; ODC-Az
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P54368
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Expression Region
Phe95~Glu219
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Molecular Weight
44kDa
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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
OAZ1, or ornithine decarboxylase antizyme 1, is a critical regulatory protein involved in polyamine metabolism, which is essential for cellular growth, differentiation, and proliferation. The study of OAZ1 is particularly relevant in the context of cancer research, as altered polyamine levels are often associated with tumorigenesis and tumor progression. OAZ1 functions by inhibiting ornithine decarboxylase (ODC), the enzyme responsible for the synthesis of polyamines, such as putrescine, spermidine, and spermine. When OAZ1 is expressed, it forms a complex with ODC, leading to the degradation of ODC and a consequent decrease in polyamine production. This mechanism highlights OAZ1’s role as a tumor suppressor protein. Additionally, recent research has suggested that OAZ1 may have implications in regulating various cellular processes beyond polyamine metabolism, including apoptosis and gene expression. Understanding the structure and function of OAZ1 can provide insights into its potential as a therapeutic target, as manipulating its expression or activity could offer novel strategies for cancer treatment. Furthermore, exploring the interaction networks and pathways associated with OAZ1 will enhance our comprehension of its diverse roles in cellular physiology and pathology. Given the growing interest in the interplay between polyamines and cellular signaling mechanisms, the investigation of OAZ1 continues to be an important area of research with potential implications for cancer therapeutics and biotechnology.
