Anti-Human OAZ1 Antibody Pair

Product Description: Ornithine decarboxylase antizyme 1 (OAZ1) is a regulatory protein that plays a crucial role in controlling intracellular polyamine levels by negatively regulating ornithine decarboxylase (ODC) activity and polyamine uptake, thereby influencing cell growth and proliferation. OAZ1 is widely expressed in human tissues and is part of the antizyme family, which modulates polyamine biosynthesis through a unique mechanism involving ribosomal frameshifting in response to polyamine concentrations, ensuring the production of functional antizyme only when polyamine levels are high. Structurally, OAZ1 binds to ODC, targeting it for proteasomal degradation, and its interaction with ODC is influenced by specific amino acid residues, as demonstrated by mutagenesis studies. In terms of disease relevance, OAZ1 has been shown to inhibit proliferation and induce differentiation in certain cancer cells, such as oral cancer, suggesting a potential tumor-suppressive role by limiting excessive polyamine-driven cell growth. Protein Function: 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) [The Uniprot Consortium]