HIV-1 Rev 34-50

HIV-1 Rev (34-50) is a 17-aa peptide derived from the Rev-responsive element (RRE)-binding domains of Rev in HIV-1, with anti-HIV-1 activity.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R1429

CAS No:141237-50-5

Synonyms/Alias:HIV-1 rev Protein (34-50)

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M.F/Formula
C₉₇H₁₇₃N₅₁O₂₄
M.W/Mr.
2437.74
Sequence
One Letter Code: TRQARRNRRRRWRERQR
three Letter Code: Thr-Arg-Gln-Ala-Arg-Arg-Asn-Arg-Arg-Arg-Arg-Trp-Arg-Glu-Arg-Gln-Arg

HIV-1 Rev 34-50 is a synthetic peptide fragment derived from the Rev protein of Human Immunodeficiency Virus type 1 (HIV-1), specifically encompassing amino acids 34 to 50 of the full-length protein. As a critical domain of the Rev protein, this peptide segment is known for its involvement in nuclear export of viral RNA, a process essential for HIV-1 replication and gene expression. The 34-50 region contains part of the arginine-rich motif, which is vital for RNA binding and nuclear localization, making it a focal point for studies investigating HIV-1 molecular biology, host-pathogen interactions, and the development of antiviral strategies. Its defined sequence and biochemical properties provide researchers with a valuable tool for dissecting the mechanistic underpinnings of Rev-mediated RNA transport and for exploring potential intervention points in the viral life cycle.

Molecular interaction studies: The HIV-1 Rev 34-50 peptide is widely utilized in molecular biology research to probe the interactions between the Rev protein and its RNA targets, particularly the Rev response element (RRE). By isolating this functional domain, researchers can precisely map binding sites, quantify affinity constants, and elucidate the structural determinants required for high-specificity RNA recognition. Such studies are fundamental for understanding how the Rev protein orchestrates the export of unspliced and partially spliced viral RNAs from the nucleus to the cytoplasm, a process pivotal for productive HIV-1 infection.

Structural and biophysical analysis: The defined sequence of the Rev 34-50 fragment enables detailed structural investigations using techniques such as nuclear magnetic resonance (NMR) spectroscopy, X-ray crystallography, and circular dichroism (CD) spectroscopy. These analyses provide insights into the secondary structure, conformational dynamics, and folding properties of the Rev arginine-rich motif. By studying this peptide in isolation or in complex with nucleic acids, scientists gain a deeper understanding of the molecular basis for Rev's function and the role of peptide structure in mediating protein-RNA interactions.

Peptide-based inhibitor development: The functional relevance of the Rev 34-50 region in RNA binding and nuclear localization renders it an attractive template for the rational design of peptide-based inhibitors. Researchers can use this peptide as a starting point for developing analogs or mimetics that disrupt Rev-RRE interactions, thereby interfering with viral RNA export. Such efforts contribute to the discovery and optimization of novel molecular probes and potential antiviral agents targeting the HIV-1 replication machinery at the level of nucleocytoplasmic transport.

Cellular trafficking assays: In cell-based experimental systems, the HIV-1 Rev 34-50 peptide serves as a model substrate to investigate nuclear import and export pathways. By conjugating this peptide to fluorescent tags or other reporter molecules, researchers can visualize and quantify the nuclear localization signals (NLS) and nuclear export signals (NES) embedded within the Rev protein. These assays are instrumental in characterizing the cellular machinery involved in nucleocytoplasmic trafficking and in validating the specificity of transport mechanisms that HIV-1 exploits.

Antibody production and epitope mapping: The 34-50 amino acid region of the HIV-1 Rev protein is frequently employed as an immunogen for the generation of polyclonal or monoclonal antibodies. Its unique sequence and surface accessibility make it suitable for raising antibodies that recognize native or denatured forms of the Rev protein. These antibodies are valuable tools for immunodetection, immunoprecipitation, and epitope mapping studies, facilitating the analysis of Rev expression, localization, and function in diverse experimental contexts.

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