ADO anticorps
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- Antigène Voir toutes ADO Anticorps
- ADO (2-Aminoethanethiol (Cysteamine) Dioxygenase (ADO))
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Reactivité
- Humain, Souris, Rat
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Hôte
- Lapin
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Clonalité
- Polyclonal
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Conjugué
- Cet anticorp ADO est non-conjugé
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Application
- Western Blotting (WB), Flow Cytometry (FACS)
- Purification
- Antigen affinity purified
- Immunogène
- Amino acids E49-E261 from the human protein were used as the immunogen for the ADO antibody.
- Isotype
- IgG
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- Indications d'application
- Western blot: 0.5-1 μg/mL,FACS: 1-3 μg/10^6 cells
- Restrictions
- For Research Use only
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- Buffer
- 0.5 mg/mL if reconstituted with 0.2 mL sterile DI water
- Stock
- -20 °C
- Stockage commentaire
- After reconstitution, the ADO antibody can be stored for up to one month at 4°C. For long-term, aliquot and store at -20°C. Avoid repeated freezing and thawing.
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- Antigène
- ADO (2-Aminoethanethiol (Cysteamine) Dioxygenase (ADO))
- Autre désignation
- ADO / 2-Aminoethanethiol dioxygenase (ADO Produits)
- Synonymes
- anticorps C10orf22, anticorps Gm237, anticorps RGD1308233, anticorps wu:fc32g01, anticorps wu:fc52c12, anticorps zgc:101580, anticorps 2-aminoethanethiol dioxygenase, anticorps 2-aminoethanethiol (cysteamine) dioxygenase, anticorps 2-aminoethanethiol (cysteamine) dioxygenase a, anticorps ADO, anticorps Ado, anticorps LOC100351598, anticorps adoa
- Sujet
- Human thiol dioxygenases include cysteine dioxygenase (CDO) and cysteamine (2-aminoethanethiol) dioxygenase (ADO). CDO adds 2 oxygen atoms to free cysteine, whereas ADO adds 2 oxygen atoms to free cysteamine to form hypotaurine. It is demonstrated that 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. It is also noted that 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.
- UniProt
- Q96SZ5
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