GP(33-41), a 9-aa-long peptide, is the optimal sequence of the GP1 epitope of lymphocytic choriomeningitis virus, and can upregulate H-2Db molecules at the RMA-S (Db Kb) cell surface with SC50 of 344 nM.
CAT No: R1394
GP(33-41) is a synthetic peptide fragment corresponding to residues 33 through 41 of the lymphocytic choriomeningitis virus glycoprotein (LCMV GP). As a well-defined model epitope, this nonapeptide is widely recognized for its immunological significance in T cell research, particularly in studies involving major histocompatibility complex (MHC) class I-restricted antigen presentation. Its precise sequence and established immunogenic properties make it an indispensable reagent in immunology, cellular biology, and peptide-based assay development. Researchers utilize GP(33-41) to dissect the mechanisms of antigen recognition, T cell activation, and immune response modulation, contributing to a deeper understanding of host-pathogen interactions and adaptive immunity.
Epitope mapping: The peptide serves as a gold-standard model antigen for epitope mapping studies, particularly in the context of CD8+ T cell recognition. By providing a defined sequence that interacts specifically with H-2Db MHC class I molecules, it enables researchers to characterize T cell receptor (TCR) specificity, affinity, and cross-reactivity. This capability is essential for elucidating the molecular basis of antigen recognition and for the rational design of immunological assays or engineered T cell receptors.
Immune response monitoring: As a canonical cytotoxic T lymphocyte (CTL) epitope, GP(33-41) is frequently employed to monitor antigen-specific T cell responses in murine models of viral infection and immunization. Its use in peptide stimulation assays, such as ELISPOT and intracellular cytokine staining, allows for the quantification and functional analysis of GP-specific CD8+ T cells. These applications provide critical insights into the dynamics of antiviral immunity, immunodominance hierarchies, and memory T cell formation.
Peptide-MHC complex generation: The defined sequence and high affinity of this peptide for H-2Db facilitate the in vitro assembly of peptide-MHC complexes. Such complexes are instrumental in generating MHC tetramers or multimers used for the direct detection and isolation of antigen-specific T cells via flow cytometry. This approach supports advanced immunophenotyping, functional profiling, and the study of T cell repertoire diversity in various experimental settings.
Vaccine research: The immunodominant characteristics of GP(33-41) make it a valuable tool in preclinical vaccine development and immunogenicity assessment. By serving as a reference antigen in vaccination studies, the peptide helps evaluate the efficacy of candidate vaccines in eliciting robust CTL responses. Its application in comparative immunogenicity assays aids in optimizing vaccine formulations and delivery strategies aimed at enhancing cellular immunity.
Antigen processing studies: Researchers utilize GP(33-41) to investigate the mechanisms underlying antigen processing and presentation by antigen-presenting cells (APCs). By analyzing how the peptide is generated, transported, and loaded onto MHC class I molecules, scientists can dissect the cellular pathways that govern immune surveillance and pathogen recognition. These studies contribute to a broader understanding of immune system function and inform the development of novel immunotherapeutic strategies.
1. TMEM16F and dynamins control expansive plasma membrane reservoirs
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