PNC-27

PNC-27 is a 32-residue chimeric peptide that fuses a p53-derived segment (the HDM-2-binding domain, p53 residues 12–26) to a penetratin membrane-residency sequence derived from the Antennapedia homeodomain. Investigators study it as a structurally defined research material in cancer-cell-biology models focused on p53 / HDM-2 interaction and membrane-associated cell research. The peer-reviewed literature catalogs PNC-27 in cell-membrane research and in comparative structure-activity work on p53-domain chimeric peptides. Its molecular identity is fixed by structural confirmation against PubChem CID 16201774, empirical formula C188H293N53O44S. The reference material supplied here is intended for laboratory characterization and in-vitro cell-model studies only. For research use only; not for human consumption, medical use, or veterinary application.

PNC-27 combines two functional modules documented across the published literature: an N-terminal p53-derived segment spanning the HDM-2-binding residues, and a C-terminal penetratin sequence that confers membrane association and intracellular access. The literature describes the chimeric peptide as engaging membrane-associated HDM-2 in research models, with the penetratin module driving the peptide’s documented localization to the cell membrane. Because the documented point of interaction is a protein-protein interface rather than a receptor cascade, the interaction profile is framed in terms of binding and membrane-residency behavior in cell research. Its relatively large size and single cysteine are consistent with the reported empirical formula C188H293N53O44S. All activity descriptors here are framed as documented in published research rather than as effects of the supplied product. Structural confirmation is established by mass spectrometry and HPLC-validated purity on each Certificate of Analysis.

Experimental domains documented in the published literature include p53 / HDM-2 protein-interaction studies, cancer-cell-membrane research, cell-penetrating-peptide localization assays using the penetratin module, comparative structure-activity work on p53-domain chimeric peptides, and mechanism studies distinguishing membrane-associated from nuclear p53-pathway research. Investigators use PNC-27 research material as a defined p53-domain / penetratin chimeric reference. Use in laboratory research extends to mechanism-elucidation paradigms probing membrane-associated protein-interaction biology. The reference standard is supplied for these and equivalent in-vitro experimental contexts only, with no associated guidance for human, clinical, or veterinary use.

Each lot is characterized by reverse-phase HPLC for chromatographic purity and by mass spectrometry for molecular-ion confirmation against the C188H293N53O44S empirical formula — an important check given the peptide’s 32-residue length, where truncation and deletion sequences are the principal purity concern. Purity is reported as an HPLC-area percentage on the Certificate of Analysis distributed with every lot, alongside the molecular-weight match within instrument tolerance. Peptide content is determined by amino-acid analysis or nitrogen-content assay following the analytical method specified on the COA. Residual solvent and water content are reported categorically when these parameters are part of the lot release specification. The COA records the lot identifier, manufacturing date, and analytical method versions used, providing a traceable provenance chain from synthesis through release. Researchers requiring batch-level analytical detail should reference the COA distributed with the supplied material.

For laboratory storage, the lyophilized reference standard should be held at −20°C in its sealed, light-protected container until ready for analytical use. Allow vials to equilibrate to ambient temperature before opening to avoid moisture condensation on the lyophile. Reconstitution for in-vitro experimental use is typically performed in bacteriostatic water or a researcher-selected buffer compatible with the downstream assay; the single cysteine residue can participate in oxidation, so avoid strong oxidizing conditions unless required by the assay. Once reconstituted, store the working solution at 2–8°C and characterize stability in the relevant buffer prior to extended storage. Avoid repeated freeze-thaw cycles of reconstituted material — single-use aliquots are preferred where peptide integrity is assay-critical. These handling parameters reflect general best-practice for lyophilized peptide reference standards and do not constitute preparation guidance for human or veterinary use.