Monoclonal Anti-Ornithine Decarboxylase (ODC) antibody produced in mouse

Monoclonal Anti-Ornithine Decarboxylase (ODC) (mouse IgG2b isotype) is derived from the ODC-29 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from immunized BALB/c mice. Its amino acid sequence is well conserved among species; the overall identity of the amino acid sequences of mouse, rat and human ODC proteins is greater than 90%.

Ornithine decarboxylase (ODC) levels increase rapidly after implantation during mouse embryogenesis. The gene encoding this protein is localized on mouse chromosome 12 and human chromosome 2.

By immunohistochemical staining of formalin-fixed, paraffin-embedded human prostate and colon carcinoma, the labeling is confined to epithelial cells.

recombinant mouse ornithine decarboxylase.

Monoclonal Anti-Ornithine Decarboxylase (ODC) antibody produced in mouse has been used in Western blotting.

Monoclonal Anti-Ornithine Decarboxylase (ODC) has also been used in enzyme linked immunosorbent assay (ELISA), immunoprecipitation, immunoblotting and immunohistochemistry.

Ornithine Decarboxylase (ODC) biological activity is rapidly induced to promote cell proliferation in response to hormones, drugs, growth factors, mitogens and tumour promoters. ODC mRNA levels are also elevated in transformed cells including lung carcinomas and human colon adenomas and carcinomas. ODC activity in colorectal carcinomas has been shown to be greater than that in adenomas, which, in turn, is greater than that of normal mucosa. ODC has a half-life of 8-30 min, the shortest half-life time reported in eukaryotic cells.

Ornithine decarboxylase (ODC) converts L-ornithine to putrescine. It has a role in cell replication. ODC is also involved in the polyamine synthesis pathway. The protein is upregulated in cancers. Overexpression of ODC has been associated with carcinogenesis in mice.

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