Indoleamine 2,3-dioxygenase 1
Indoleamine 2,3-dioxygenase 1 (199-207) is a synthetic peptide fragment corresponding to residues 199 through 207 of the human IDO1 enzyme. As a defined sequence peptide, it serves as a valuable molecular tool for studies focusing on the immunoregulatory and metabolic functions of indoleamine 2,3-dioxygenase 1, a key enzyme involved in tryptophan catabolism and immune modulation. The 199-207 region is of particular interest due to its potential involvement in enzyme activity, structural conformation, and recognition by immune effector molecules. Researchers utilize this peptide to dissect specific protein-protein interactions, study post-translational modifications, and develop analytical assays targeting IDO1-related pathways.
Epitope mapping: In immunological research, the 199-207 peptide fragment is frequently employed to identify and characterize epitopes recognized by T cells or antibodies. By using this defined sequence in in vitro assays, investigators can pinpoint the immune-dominant regions of IDO1 relevant to antigen presentation and immune recognition. Such studies are crucial for understanding how IDO1 contributes to immune tolerance, autoimmunity, or tumor immune escape, and the 199-207 fragment provides a precise tool for dissecting these mechanisms at the peptide level.
Peptide-based assay development: The defined sequence of the IDO1 (199-207) peptide makes it suitable for use as a standard or control in various biochemical and immunological assays. It can be incorporated into ELISA, mass spectrometry, or multiplex platforms to quantify immune responses, validate antibody specificity, or calibrate detection systems. Its well-characterized structure supports the development of robust, reproducible assays for monitoring IDO1 activity or presence in research samples.
Protein-protein interaction studies: As a segment of the full-length IDO1 protein, the 199-207 peptide can be used to probe specific binding interactions with other proteins, small molecules, or nucleic acids. By immobilizing or labeling the peptide, researchers can screen for potential binding partners, map interaction domains, or study competitive inhibition within the IDO1 pathway. Such applications are essential for elucidating the molecular mechanisms that regulate tryptophan metabolism and immune signaling.
Post-translational modification analysis: The 199-207 region of IDO1 may contain residues susceptible to post-translational modifications, such as phosphorylation or ubiquitination. Synthetic peptides corresponding to this region allow for detailed in vitro studies of modification patterns, enzymatic specificity, and functional consequences. By utilizing this peptide in modification assays, scientists can gain insight into how regulatory processes affect IDO1 function and stability.
Peptide immunization and tolerance models: The IDO1 (199-207) peptide is also used in experimental immunization protocols to generate peptide-specific T cell responses or to induce tolerance in model systems. These applications enable researchers to explore the immunogenicity of IDO1-derived sequences, assess the potential for immune modulation, and investigate the mechanisms underlying antigen-specific tolerance or activation. Such studies are foundational for advancing knowledge of immune regulation in the context of IDO1 biology.
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