ORF2(81-102) is a peptide fragment derived from an open-reading-frame region enriched in polar and charged residues. The sequence supports investigation of local folding, transient secondary structures, and partner recognition motifs. Researchers use it to explore peptide-protein interfaces and solvent-dependent conformational shifts. Its defined boundaries enable controlled biophysical and structural analyses.
CAT No: ta-433
ORF2(81-102) is a synthetic peptide fragment corresponding to amino acid residues 81 through 102 of the open reading frame 2 (ORF2) protein, typically derived from viral or microbial sources such as hepatitis E virus (HEV). As a defined peptide sequence, it is widely recognized for its significance in molecular virology, immunology, and protein interaction studies. The unique segment encompasses critical epitopes and structural motifs that contribute to the biological function of the full-length ORF2 protein, making it an essential tool for researchers investigating viral assembly, host-pathogen interactions, and immune recognition mechanisms.
Epitope mapping: In immunological research, the ORF2(81-102) peptide is frequently utilized for precise epitope mapping. Its defined sequence allows scientists to identify and characterize linear B-cell or T-cell epitopes within the ORF2 region, facilitating the development of serological assays and the study of antigen-antibody interactions. Through such mapping, researchers can gain insights into the immunodominant areas of the ORF2 protein, which are critical for understanding host immune responses and for the rational design of diagnostic reagents.
Antibody production: The peptide serves as an effective immunogen for generating sequence-specific polyclonal or monoclonal antibodies. By conjugating ORF2(81-102) to suitable carrier proteins, it can elicit targeted immune responses in laboratory animals, leading to the production of antibodies that recognize the native ORF2 protein or its fragments. These antibodies are invaluable for applications such as western blotting, immunoprecipitation, and immunofluorescence, where specificity for particular epitopes is required.
Protein-protein interaction studies: Researchers leverage the ORF2(81-102) peptide to dissect protein-protein interactions that involve the ORF2 protein. In vitro binding assays, such as peptide pull-downs or surface plasmon resonance, employ this fragment to identify host or viral factors that interact with the ORF2 region. Understanding these molecular interactions is fundamental for elucidating viral replication mechanisms, host adaptation, and the identification of potential antiviral targets.
Structural biology: The defined sequence of ORF2(81-102) makes it suitable for structural analyses, including nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography. By studying the isolated peptide, scientists can investigate its secondary structure, conformational dynamics, and potential for forming biologically relevant motifs. Such structural insights contribute to a deeper understanding of how the ORF2 protein folds, assembles, and functions within the viral life cycle.
Peptide-based assay development: The ORF2(81-102) fragment is also employed in the development of sensitive and specific assays for viral detection or quantification. Its incorporation into enzyme-linked immunosorbent assays (ELISA) or other immunoassay platforms enables the selective capture or detection of antibodies directed against the ORF2 protein in biological samples. This application supports both basic research and epidemiological studies by providing reliable tools for monitoring infection or immune status in experimental systems.
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