Specification
    
        | Organism | Sus scrofa (Pig) | 
| Expression Host | E.coli | 
| Protein Tag | N-terminal MBP-tagged and C-terminal 6xHis-Avi-tagged | 
| Purity | Greater than 85% as determined by SDS-PAGE. | 
| Endotoxin Level | Not test. | 
| Biological Activity | |
| Uniprot ID | P53603 | 
| Gene Names | FTCD | 
| Alternative Names | (Formiminotransferase-cyclodeaminase)(FTCD)(Glutamate formimidoyltransferase)(Glutamate formiminotransferase)(Glutamate formyltransferase)(Formimidoyltetrahydrofolate cyclodeaminase)(Formiminotetrahydrofolate cyclodeaminase) | 
| Expression Region | 1-326aa | 
| Product Form | Liquid or Lyophilized powder | 
| Buffer | The default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol if the delivery form is liquid. The lyophilization buffer is Tris/PBS-based buffer, 6% Trehalose, pH 8.84 if the delivery form is lyophilized powder. Please contact us if you have any special requirment. | 
| Reconstitution | Please reconstitute protein in deionized sterile water and we recommend that briefly centrifuge thevial prior to opening the vial .We recommend aliquot for long-term storage at -20℃/-176℃. | 
| Protein Length | Partial | 
| Molecular Weight | 83.7 kDa | 
| Protein Sequence | MSQLVECVPNFSEGKNQEVIDAISRAVAQTPGCVLLDVDSGPSTNRTVYTFVGRPEDVVEGALNAARAAYQLIDMSRHHGEHPRMGALDVCPFIPVRGVTMDECVRCAQAFGQRLAEELGVPVYLYGEAARTAGRQSLPALRAGEYEALPEKLKQAEWAPDFGPSAFVPSWGATVAGARKFLLAFNINLLSTREQAHRIALDLREQGRGKDQPGRLKKVQAIGWYLDEKNLAQVSTNLLDFEVTGLHTVFEETCREAQELSLPVVGSQLVGLVPLKALLDAAAFYCEKENLFLLQDEHRIRLVVNRLGLDSLAPFKPKERIIEYLV | 
        Background
    
        | Research Areas | Metabolism | 
| Relevance | Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool.; Binds and promotes bundling of vimentin filaments originating from the Golgi. | 
| Function | |
| Reference | "The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme." Kohls D, Sulea T, Purisima EO, MacKenzie RE, Vrielink A. Structure 8 35-46 (2000) | 
        QC Data
    
        | Note | Please contact us for QC Data | 
| Product Image (Reference Only) |  | 
 
