Recombinant Mouse Tryptophan 2,3-dioxygenase(Tdo2) CSB-EP023351MO
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
Tryptamin 2,3-dioxygenase (Tryptophan oxygenase) (TO) (TRPO) (Tryptophan pyrrolase) (Tryptophanase) (TDO) (Tdo)
Species: (Organism)
Mus musculus (Mouse)
Gene Names:
Tdo2
Tag info:
N-terminal 6xHis-tagged
Target Protein AA Sequence:
MSGCPFAGNSVGYTLKNVSMEDNEEDRAQTGVNRASKGGLIYGNYLQLEKILNAQELQSEVKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVIARMHRVVVIFKLLVQQFSVLETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQSLRVPYNRKHYRDNFGGDYNELLLKSEQEQTLLQLVEAWLERTPGLEPNGFNFWGKFEKNILKGLEEEFLRIQAKTDSEEKEEQMAEFRKQKEVLLCLFDEKRHDYLLSKGERRLSYRALQGALMIYFYREEPRFQVPFQLLTSLMDIDTLMTKWRYNHVCMVHRMLGTKAGTGGSSGYHYLRSTVSDRYKVFVDLFNLSTYLVPRHWVPKMNPIIHKFLYTAEYSDSSYFSSDESD
Expression Region:
1-406aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Full Length
Pathway:
Mol. Weight:
53.3 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:
Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.
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:
"STAT3 down-regulates the expression of cyclin D during liver development." Matsui T., Kinoshita T., Hirano T., Yokota T., Miyajima A. J. Biol. Chem. 277:36167-36173(2002)
