Human CDO1 protein (Recombinant) (His-Tag) (STJP016535)
SPECIFICATIONS
HostE.coli
ImmunogenHuman
General Information
| Short Description | Recombinant-Human CDO1-His-Tag protein was developed from e.coli and has a target region of His-Tag. For use in research applications. |
| Applications | SDS-PAGE |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Concentration | 1 mg/mL |
| Formulation | Liquid in 20mM Tris-HCl buffer (pH 8.0) containing 10% Glycerol, 1mM DTT |
| Storage Instruction | For short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles. |
Target Information
| Gene Symbol | CDO1 |
| Gene ID | 1036 |
| Uniprot ID | CDO1_HUMAN |
| Accession Number | AAH_24241 |
| Immunogen | Human |
| Immunogen Region | 1-170aa |
| Immunogen Sequence | MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMEQ TEVLKPRTLA DLIRILHQLF AGDEVNVEEV QAIMEAYESD PTEWAMYAKF DQYRYTRNLV DQGNGKFNLM ILCWGEGHGS SIHDHTNSHC FLKMLQGNLK ETLFAWPDKK SNEMVKKSER VLRENQCAYI NDSVGLHRVE NISHTEPAVS LHLYSPPFDT CHAFDQR |
Additional Info
| Tissue Specificity | Highly expressed in liver and placenta. Low expression in heart, brain and pancreas. Also detected in hepatoblastoma Hep-G2 cells. |
| Post Translational Modifications | The thioether cross-link between Cys-93 and Tyr-157 plays a structural role through stabilizing the Fe(2+) ion, and prevents the production of highly damaging free hydroxyl radicals by holding the oxygen radical via hydroxyl hydrogen. |
| Function | Catalyzes the oxidation of cysteine to cysteine sulfinic acid with addition of molecular dioxygen. |
| Protein Name | Cysteine Dioxygenase Type 1Cysteine Dioxygenase Type ICdoCdo-I |
| Database Links | Reactome: R-HSA-1614558 |
| Cellular Localisation | |
| Alternative Protein Names | Cysteine Dioxygenase Type 1 proteinCysteine Dioxygenase Type I proteinCdo proteinCdo-I proteinCDO1 protein |
Information sourced from Uniprot.org