Influenza HA (110 – 119) CAS NO.132031-50-6

The biological function of Influenza HA (110-119) is defined by its specific interaction with the Major Histocompatibility Complex class II (MHC II) molecule, particularly the H-2I-Ed allele, forming a peptide-MHC complex that is recognized by the T-cell receptor (TCR) on CD4+ helper T-cells. Unlike internal viral proteins that typically trigger MHC I restricted cytotoxic responses, this extracellular HA-derived fragment is processed and presented on the surface of antigen-presenting cells (APCs) like dendritic cells to engage the CD4+ T-cell compartment. Notably, this specific epitope possesses the unique capacity to selectively stimulate the proliferation and activation of CD4+ CD25+ Regulatory T cells (Tregs), which in turn exert suppressive functions on effector T-cell responses, thereby influencing the fine-tuning of the overall immune balance and preventing excessive immunopathology during viral encounters.

This product is indicated for preclinical research applications targeting professionals in viral immunology, autoimmune research, and vaccine technology who are investigating the nuances of CD4+ T-cell epitope mapping and immune regulation. It is particularly suitable for researchers utilizing the peptide to pulse bone marrow-derived dendritic cells or splenocytes to study antigen presentation dynamics, to isolate and expand influenza-specific T-cell lines, or to model immune tolerance mechanisms in vitro. Furthermore, it is applicable for scientists conducting structure-activity relationship studies on HA epitopes, serving as a standard for ELISA coating to detect HA-specific antibodies, and for pharmacologists testing immunomodulatory drugs that aim to manipulate Treg function or Th cell differentiation, all within controlled laboratory environments.

As a raw synthetic peptide reagent not formulated for human therapeutic or diagnostic administration, Influenza HA (110-119) does not possess approved clinical efficacy, yet it is fundamental in elucidating immune correlates validated in extensive preclinical and clinical immunological studies. Experimental data confirm that HA-specific CD4+ T-cells recognize this epitope across different influenza strains, and that analogs of this peptide can enhance T-cell activation by modifying dendritic cell antigen presentation functions or activate Treg suppressor mechanisms. Additionally, research highlights its utility in dissecting why certain HA epitopes induce tolerance versus immunity, underscing its value as a benchmark tool for measuring CD4+ T-cell memory, designing adjuvanted vaccines that optimize T-helper responses, and developing peptide-based immunotherapies for autoimmune conditions rather than acting as a standalone clinical treatment.

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