The Recombinant Human IDO-1 Protein is a biologically active recombinant protein that plays a significant role in various cellular processes and signaling pathways in human biology. This protein is widely employed in immunological research, cell biology studies, protein-protein interaction analyses, and therapeutic development, providing researchers with a reliable tool for investigating IDO-1 function and its implications in health and disease.
This product (SKU: RPCB0140) is produced using E. coli and features a No tag tag for convenient detection and purification. The protein exhibits a calculated molecular weight of 45.19 kDa with an observed molecular weight of 45 kDa under denaturing conditions, achieving ≥ 95 % as determined by SDS-PAGE., ensuring exceptional quality and consistency for research applications.
High quality, high purity and low endotoxin recombinant Recombinant Human IDO-1 Protein (RPCB0140), tested reactivity in E. coli and has been validated in SDS-PAGE.100% guaranteed.
Endotoxin:
< 0.1 EU/μg of the protein by LAL method.
Purity:
≥ 95 % as determined by SDS-PAGE.
Formulation:
Lyophilized from a 0.22 μm filtered solution of 50mM Tris, 150mM NaCl, pH 8.0.Contact us for customized product form or formulation.
Reconstitution:
Centrifuge the vial before opening. Reconstitute to a concentration of 0.1-0.5 mg/mL in sterile distilled water. Avoid vortex or vigorously pipetting the protein. For long term storage, it is recommended to add a carrier protein or stablizer (e.g. 0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose), and aliquot the reconstituted protein solution to minimize free-thaw cycles.
Storage:
Store at -20℃.Store the lyophilized protein at -20℃ to -80 ℃ up to 1 year from the date of receipt. After reconstitution, the protein solution is stable at -20℃ for 3 months, at 2-8℃ for up to 1 week.
Indoleamine 2,3-dioxygenase (IDO) is a heme enzyme that catalyzes the first and rate-limiting step in tryptophan catabolism to N-formyl-kynurenine. This enzyme acts on multiple tryptophan substrates including D-tryptophan, L-tryptophan, 5-hydroxy-tryptophan, tryptamine, and serotonin. This enzyme is thought to play a role in a variety of pathophysiological processes such as antimicrobial and antitumor defense, neuropathology, immunoregulation, and antioxidant activity. Through its expression in dendritic cells, monocytes, and macrophages this enzyme modulates T-cell behavior by its peri-cellular catabolization of the essential amino acid tryptophan.
Recombinant Human IDO-1 Protein was determined by SDS-PAGE under reducing conditions with Coomassie Blue.
