Recombinant Human OAZ1 protein is a Human Full Length protein, in the 1 to 228 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, MS.
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Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimer, and targets the monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome (PubMed:17900240, PubMed:26305948, PubMed:26443277). Triggers ODC degradation by inducing the exposure of a cryptic proteasome-interacting surface of ODC (PubMed:26305948). Stabilizes AZIN2 by interfering with its ubiquitination (PubMed:17900240). Also inhibits cellular uptake of polyamines by inactivating the polyamine uptake transporter. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. Involved in the translocation of AZIN2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol (PubMed:12097147).
OAZ, OAZ1, Ornithine decarboxylase antizyme 1, AZ1, ODC-Az
Recombinant Human OAZ1 protein is a Human Full Length protein, in the 1 to 228 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 30% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab131694 was purified using conventional chromatography techniques.
Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimer, and targets the monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome (PubMed:17900240, PubMed:26305948, PubMed:26443277). Triggers ODC degradation by inducing the exposure of a cryptic proteasome-interacting surface of ODC (PubMed:26305948). Stabilizes AZIN2 by interfering with its ubiquitination (PubMed:17900240). Also inhibits cellular uptake of polyamines by inactivating the polyamine uptake transporter. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. Involved in the translocation of AZIN2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol (PubMed:12097147).
Belongs to the ODC antizyme family.
OAZ1 also known as Ornithine Decarboxylase Antizyme 1 is a regulatory protein with a mass of approximately 27 kDa. It functions to inhibit ornithine decarboxylase (ODC) an enzyme that plays a role in the biosynthesis of polyamines. These polyamines are important for cell growth and differentiation. OAZ1 is widely expressed in various tissues including liver kidney and brain indicating its broad regulatory role in cellular function.
OAZ1 acts as an essential part of the polyamine homeostasis by regulating the degradation of ornithine decarboxylase. This regulation occurs through binding to ODC targeting it for degradation by the 26S proteasome and preventing its activity. OAZ1 does not form a larger protein complex but it plays an important role in controlling polyamine levels which are critical for many cellular functions such as DNA stabilization and transcription.
OAZ1 integrates into the polyamine biosynthesis and catabolism pathways. Its inhibitory function on ODC plays a significant role in maintaining polyamine balance. This activity places OAZ1 in relationship with other proteins like antizyme inhibitor 1 (AZIN1) which modulates OAZ1 activity by binding and reducing its inhibitory effect on ODC. OAZ1's function connects with the broader network of protein catabolism pathways that regulate cellular proliferation.
OAZ1 holds significance in conditions related to polyamine dysregulation including cancer and neurological disorders. In cancer the overexpression of ODC can lead to excessive cell growth while OAZ1 helps in suppressing this by promoting ODC degradation. In neurodegenerative diseases altered polyamine metabolism involving OAZ1 may influence pathogenesis. Its interaction with ODC and AZIN1 factors into these disease processes highlighting OAZ1's role in maintaining cellular health in both normal and diseased states.
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15% SDS PAGE analysis of 3 μg of ab131694.
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