The ADO Antibody (PAC017495) is a polyclonal antibody designed for research involving ADO, a cell surface molecule with immunomodulatory functions. The antibody, raised in rabbits, is highly reactive with human samples and is validated for use in various applications, including Western blot and immunohistochemistry.ADO, also known as adenosine deaminase, is involved in regulating immune responses and inflammation by modulating the levels of adenosine, a potent immunosuppressive molecule. Its role in immune regulation makes it a promising target for studies in immunology and cancer research. By detecting and analyzing ADO protein levels in different cell types, researchers can gain valuable insights into its functions and potential therapeutic applications.
Furthermore, ADO has been implicated in various diseases, including cancer, inflammatory disorders, and autoimmune conditions. Understanding the mechanisms underlying ADO's immunomodulatory effects is essential for developing targeted therapies that can manipulate immune responses and potentially treat these diseases effectively. The ADO Antibody (PAC017495) is a valuable tool for researchers seeking to elucidate the role of ADO in health and disease.
Gel: 10%SDS-PAGE, Lysate: 30 μg, Lane: Mouse testis tissue, Primary antibody: PACO17495(ADO Antibody) at dilution 1/1200, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 30 minutes.
The image on the left is immunohistochemistry of paraffin-embedded Human liver cancer tissue using PACO17495(ADO Antibody) at dilution 1/30, on the right is treated with synthetic peptide. (Original magnification: x200).
Background:
Human thiol dioxygenases include cysteine dioxygenase (CDO, MIM 603943) and cysteamine (2-aminoethanethiol) dioxygenase (ADO, EC 1.13.11.19). CDO adds 2 oxygen atoms to free cysteine, whereas ADO adds 2 oxygen atoms to free cysteamine to form hypotaurine. Mouse Ado has strong and specific dioxygenase activity in vitro towards cysteamine but not cysteine. Recombinant Ado was shown to bind iron. Overexpression of Ado in HepG2/C3A cells increased the production of hypotaurine from cysteamine. Similar results were found with human ADO. When endogenous expression of ADO was reduced by RNA-mediated interference, hypotaurine production decreased. The demonstration of high levels of ADO in brain challenges the previous assumption that most of the taurine in the brain is a consequence of CDO activity.
Synonyms:
2-aminoethanethiol (cysteamine) dioxygenase
UniProt Protein Function:
ADO:
UniProt Protein Details:
Protein type:EC 1.13.11.19; Oxidoreductase; Other Amino Acids Metabolism - taurine and hypotaurine
Chromosomal Location of Human Ortholog: 10q21.3
Cellular Component: mitochondrion
Molecular Function:metal ion binding; cysteamine dioxygenase activity
NCBI Summary:
Human thiol dioxygenases include cysteine dioxygenase (CDO; MIM 603943) and cysteamine (2-aminoethanethiol) dioxygenase (ADO; EC 1.13.11.19). CDO adds 2 oxygen atoms to free cysteine, whereas ADO adds 2 oxygen atoms to free cysteamine to form hypotaurine (Dominy et al., 2007 [PubMed 17581819]).[supplied by OMIM, Mar 2008]
