Alternative Name(s):

(Formiminotransferase-cyclodeaminase)(FTCD)(Glutamate formimidoyltransferase)(Glutamate formiminotransferase)(Glutamate formyltransferase)(Formimidoyltetrahydrofolate cyclodeaminase)(Formiminotetrahydrofolate cyclodeaminase)

Species: (Organism)

Sus scrofa (Pig)

Gene Names:

FTCD

Tag info:

N-terminal MBP-tagged and C-terminal 6xHis-Avi-tagged

Target Protein AA Sequence:

MSQLVECVPNFSEGKNQEVIDAISRAVAQTPGCVLLDVDSGPSTNRTVYTFVGRPEDVVEGALNAARAAYQLIDMSRHHGEHPRMGALDVCPFIPVRGVTMDECVRCAQAFGQRLAEELGVPVYLYGEAARTAGRQSLPALRAGEYEALPEKLKQAEWAPDFGPSAFVPSWGATVAGARKFLLAFNINLLSTREQAHRIALDLREQGRGKDQPGRLKKVQAIGWYLDEKNLAQVSTNLLDFEVTGLHTVFEETCREAQELSLPVVGSQLVGLVPLKALLDAAAFYCEKENLFLLQDEHRIRLVVNRLGLDSLAPFKPKERIIEYLV

Expression Region:

1-326aa

Subcellular Location:

Tissue Specificity:

Protein Length:

Partial

Pathway:

Mol. Weight:

83.7 kDa

Purity:

Greater than 85% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Metabolism

Function:

Involvement in disease:

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.

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

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)