Analytical Data
-
Gene name
IDO
- Application
-
Alternative Names
IDO；IDO；INDO；；Indoleamine 2.3-dioxygenase 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P14902
-
Expression Region
1-403aa
-
AA Sequence
MAHAMENSWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG
-
Molecular Weight
49.3kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The research background of IDO (indoleamine 2,3-dioxygenase) as a recombinant protein is rooted in its crucial role in immune regulation and tumor biology. IDO is an enzyme that catalyzes the degradation of tryptophan into kynurenine, an important pathway that modulates immune responses, particularly in the context of cancer and chronic infections. Elevated IDO activity has been associated with immune tolerance, allowing tumors to evade immune surveillance, thereby promoting tumor growth and metastasis. Understanding the mechanisms by which IDO contributes to immunosuppression has spurred interest in developing IDO inhibitors as novel therapeutic agents. Moreover, IDO's involvement in autoimmune diseases and neurodegenerative disorders has further broadened the scope of research surrounding this enzyme. The recombinant production of IDO proteins enables researchers to elucidate its structure-function relationship, assess its activity, and investigate potential inhibitors. Utilizing recombinant techniques also allows for the generation of modified versions of IDO that can be used in therapeutic applications or as biomarkers for disease progression. Overall, the study of IDO as a recombinant protein is significant for advancing our understanding of its biological roles and potential applications in immunotherapy and disease treatment.
