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Anti-ADO Picoband Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB |
|---|---|
| Primary Accession | Q96SZ5 |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Clonality | Polyclonal |
| Format | Lyophilized |
| Description | Rabbit IgG polyclonal antibody for 2-aminoethanethiol dioxygenase(ADO) detection. Tested with WB in Human;Mouse;Rat. |
| Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
| Gene ID | 84890 |
|---|---|
| Other Names | 2-aminoethanethiol dioxygenase, 1.13.11.19, Cysteamine dioxygenase, ADO, C10orf22 |
| Calculated MW | 29751 MW KDa |
| Application Details | Western blot, 0.1-0.5 µg/ml, Human, Mouse, Rat |
| Protein Name | 2-aminoethanethiol dioxygenase |
| Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. |
| Immunogen | E. coli-derived human ADO recombinant protein (Position: E49-E261). Human ADO shares 90.1% amino acid (aa) sequence identity with mouse ADO. |
| Purification | Immunogen affinity purified. |
| Cross Reactivity | No cross reactivity with other proteins. |
| Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
| Name | ADO |
|---|---|
| Synonyms | C10orf22 |
| Function | Plays a vital role in regulating thiol metabolism and preserving oxygen homeostasis by oxidizing the sulfur of cysteamine and N-terminal cysteine-containing proteins to their corresponding sulfinic acids using O2 as a cosubstrate (PubMed:17581819, PubMed:29752763, PubMed:31273118, PubMed:32601061). Catalyzes the oxidation of cysteamine (2-aminoethanethiol) to hypotaurine (PubMed:17581819, PubMed:29752763, PubMed:32601061). Catalyzes the oxidation of regulators of G-protein signaling 4 (RGS4) and 5 (RGS5) and interleukin-32 (IL32) (PubMed:31273118, PubMed:32601061). |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
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