HLA class II histocompatibility antigen, DO beta chain (232-240)

HLA class II histocompatibility antigen, DO beta chain (232-240) is a synthetic peptide fragment derived from the beta chain of the HLA-DO molecule, a non-classical member of the major histocompatibility complex (MHC) class II family. This peptide encompasses amino acids 232 to 240 of the DO beta subunit, a region implicated in modulating antigen presentation processes within the immune system. As HLA-DO serves as a key regulator of peptide loading onto MHC class II molecules, particularly influencing the activity of HLA-DM, this peptide segment provides a valuable tool for dissecting the structural and functional dynamics of antigen processing and presentation. Its defined sequence and immunological relevance make it a critical reagent for researchers investigating the intricacies of adaptive immunity, peptide-MHC interactions, and the molecular basis of immune recognition.

Epitope mapping: The DO beta (232-240) peptide is frequently employed in epitope mapping studies aimed at characterizing T cell recognition of MHC class II-associated peptides. By serving as a defined antigenic determinant, it enables precise identification of T cell receptor (TCR) binding sites and facilitates the assessment of peptide specificity in immune assays. Such investigations are essential for understanding the molecular underpinnings of immune surveillance and the mechanisms by which T cells discriminate between self and non-self antigens.

Peptide-MHC binding analysis: Researchers utilize this peptide in assays designed to evaluate the binding affinity and stability of peptide-MHC class II complexes. Through in vitro binding studies, the peptide supports elucidation of the structural requirements for successful peptide loading and presentation by HLA-DO and related molecules. These insights are critical for advancing knowledge of antigen processing pathways and for developing predictive models of peptide-MHC interactions, which are fundamental to immunological research and vaccine design.

Structural biology studies: The defined sequence of the DO beta (232-240) fragment makes it an ideal candidate for structural investigations, including crystallography and NMR spectroscopy. By incorporating the peptide into experimental systems, scientists can probe the conformational dynamics of peptide-MHC complexes and uncover the molecular determinants that govern antigen presentation. Such structural data provide a foundation for rational design of immunomodulatory agents and inform the development of targeted research tools.

Immunological assay development: The peptide is widely used as a control or reference antigen in the development and validation of immunological assays, such as ELISPOT, flow cytometry, and T cell proliferation assays. Its well-characterized sequence allows for standardized testing conditions, facilitating reproducible measurement of antigen-specific immune responses. This application is particularly valuable in studies seeking to benchmark assay sensitivity or to compare the immunogenicity of different peptide candidates.

Autoimmunity and tolerance research: The DO beta (232-240) peptide serves as a model antigen in investigations of immune tolerance and autoimmunity. By introducing the peptide into in vitro or ex vivo systems, researchers can examine the mechanisms by which self-peptides are processed and presented, and how these processes may contribute to the breakdown of tolerance in autoimmune conditions. Studies utilizing this peptide help clarify the delicate balance between immune activation and self-tolerance, providing insights that are fundamental to the broader field of immunology.

1. The effect of B-type allatostatin neuropeptides on crosstalk between the insect immune response and cold tolerance

2. Myotropic activity of allatostatins in tenebrionid beetles

3. An Isolated TCR αβ Restricted by HLA-A* 02: 01/CT37 Peptide Redirecting CD8+ T Cells to Kill and Secrete IFN-γ in Response to Lung Adenocarcinoma Cell Lines

4. cRGD-functionalized, DOX-conjugated, and 64Cu-labeled superparamagnetic iron oxide nanoparticles for targeted anticancer drug delivery and PET/MR imaging

5. Oleic acid and glucose regulate glucagon-like peptide 1 receptor expression in a rat pancreatic ductal cell line