Anti-OAZ1 antibody produced in rabbit

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Anti-Ornithine decarboxylase antizyme antibody produced in rabbit, Anti-ODC-Az antibody produced in rabbit
Human Protein Atlas Number:
Pricing and availability is not currently available.

biological source


Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies



product line

Prestige Antibodies® Powered by Atlas Antibodies


buffered aqueous glycerol solution

species reactivity



antibody small pack of 25 μL


immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:20-1:50

immunogen sequence




UniProt accession no.

shipped in

wet ice

storage temp.


Gene Information

human ... OAZ1(4946)

General description

OAZ1 (ornithine decarboxylase antizyme 1) is simply known as AZ1. AZ was first recognized in mammals, and is present in multiple isoforms namely, AZ1, AZ2, AZ3 and AZ4. It is a homolog of ODC enzyme with a molecular weight of 50kDa and containing 448 amino acids. It primarily exists as a monomer.


Ornithine decarboxylase antizyme recombinant protein epitope signature tag (PrEST)


All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org)and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.

Biochem/physiol Actions

OAZ1 (ornithine decarboxylase antizyme 1) forms heterodimers with ornithine decarboxylase (ODC) and thus, prevents the formation of ODC homodimers, which results in inhibition of ODC activity. Also formation of ODC-OAZ1 heterodimers facilitates 26S proteasome-mediated degradation. It regulates intracellular polyamine levels by controlling the export and import of polyamines across plasma membrane. Intestinal cell growth in the presence or absence of ODC or polyamines is directly determined by the levels of AZ1 protein. The up-regulation of this protein results in increased cell proliferation and transformation, and thus, protein might have tumorigenic roles.

Features and Benefits

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.


Corresponding Antigen APREST71204.

Physical form

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Legal Information

Prestige Antibodies is a registered trademark of Sigma-Aldrich Co. LLC


Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis
Certificate of Origin
Kuo-Liang Su et al.
The Journal of biological chemistry, 284(39), 26768-26777 (2009-07-29)
Ornithine decarboxylase (ODC) is the first enzyme involved in polyamine biosynthesis, and it catalyzes the decarboxylation of ornithine to putrescine. ODC is a dimeric enzyme, whereas antizyme inhibitor (AZI), a positive regulator of ODC that is homologous to ODC, exists...
Ramesh M Ray et al.
Amino acids, 46(9), 2231-2239 (2014-06-16)
Since antizyme (AZ) is known to inhibit cell proliferation and to increase apoptosis, the question arises as to whether these effects occur independently of polyamines. Intestinal epithelial cells (IEC-6) were grown in control medium and medium containing 5 mM difluoromethylornithine...
Bingping Wu et al.
Acta haematologica, 131(3), 141-147 (2013-11-07)
Ornithine decarboxylase antizyme (OAZ) has recently emerged as a potential therapeutic target in various malignant tumors because it plays vital roles in cellular functions including proliferation, differentiation, apoptosis and genomic stability. Therefore, there is a significant interest in discovering its...
Y Tosaka et al.
Genes to cells : devoted to molecular & cellular mechanisms, 5(4), 265-276 (2000-05-03)
Polyamines are known to play important roles in the proliferation and differentiation of many types of cells. However, in the testis, where polyamines such as spermidine and spermine exist in high concentrations, their roles still remains to be elucidated. We...
Assignment of the human antizyme gene (OAZ) to chromosome 19p13.3 by fluorescence in situ hybridization.
S Matsufuji et al.
Genomics, 38(1), 102-104 (1996-11-15)

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