Prepro VIP (81-122), human is a prepro-vasoactive intestinal polypeptide (VIP) derived peptide, corresponding to residues 81-122. Peptide histidine valine 42 (PHV-42) has been designated to correspond exactly to Prepro VIP (81-122), which reduces both the force and frequency of spontaneous contractions of isolated rat uterus.
Prepro VIP (81-122), human is a synthetic peptide fragment derived from the C-terminal region of the human preprovasoactive intestinal peptide precursor. As a bioactive peptide, it represents a specific sequence that is of significant interest in neuroendocrine research due to its relationship with the biosynthesis and maturation of vasoactive intestinal peptide (VIP), a critical neuropeptide involved in a wide array of physiological processes. The study of this peptide fragment enables researchers to dissect the molecular mechanisms governing peptide processing, neuropeptide signaling, and the regulation of neuroendocrine pathways. Its defined sequence and origin make it a valuable tool for investigations into peptide structure-function relationships and the broader context of peptide hormone biosynthesis.
Peptide processing research: Prepro VIP (81-122), human serves as a model substrate for elucidating the enzymatic cleavage events that occur during the maturation of prepropeptides into active neuropeptides. By providing this defined segment of the precursor, researchers can examine the specificity and efficiency of prohormone convertases and other proteolytic enzymes responsible for generating mature VIP. Such studies are essential for understanding the regulation of neuropeptide biosynthesis and the factors that influence peptide hormone availability within neuronal and endocrine tissues.
Structure-activity relationship studies: The availability of this peptide fragment enables detailed analysis of the structural elements required for receptor binding and biological activity. By comparing the activity of the 81-122 region with full-length VIP and other precursor-derived fragments, investigators can identify critical residues and motifs that contribute to receptor interaction, signal transduction, or stability. These insights support the rational design of peptide analogs or inhibitors for probing neuropeptide function in vitro.
Antibody development and assay calibration: The defined sequence of Prepro VIP (81-122), human makes it a useful immunogen for generating sequence-specific antibodies, which are instrumental in detecting and quantifying VIP precursor forms in biological samples. Such antibodies can be employed in immunoassays, Western blotting, or immunohistochemistry to distinguish between precursor and mature forms, facilitating studies on peptide processing dynamics and tissue-specific expression patterns.
Neuroendocrine signaling research: As a segment of the VIP precursor, this peptide provides a tool for investigating the regulation and transport of neuropeptide precursors within neural and endocrine systems. Researchers can use it to study precursor trafficking, storage, and secretion processes, as well as to probe the interactions of precursor fragments with cellular receptors or binding proteins. These applications advance the understanding of neuropeptide biosynthesis and the cellular mechanisms underlying hormone release.
Peptide synthesis and analytical method development: The defined sequence and biochemical properties of Prepro VIP (81-122), human make it a suitable standard or reference compound in peptide synthesis workflows and analytical method validation. It can be used to optimize solid-phase peptide synthesis protocols, assess chromatographic separation techniques, or calibrate mass spectrometric analyses. Such applications support the development of robust analytical platforms for peptide research and quality control in peptide manufacturing environments.
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