PNC-27 30mg
Janoshik
Batch PNC2-CA-26G-30
PNC-27
p53-Penetratin Chimeric Peptide
Also known as p53(12-26)-penetratin chimera
PNC-27 is a 32-residue chimeric peptide joining a p53-derived segment to the penetratin cell-penetrating domain, studied in oncology research for selective membrane interaction.
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This product is intended strictly for laboratory research use within the United States. It is not approved by the FDA for the diagnosis, treatment, cure, or prevention of any disease. Not for human or veterinary use.
By purchasing, you confirm the material will be used solely for lawful research purposes in accordance with applicable U.S. federal, state, and local regulations.
PNC-27 is a 32-residue chimeric peptide joining a p53-derived segment to the penetratin cell-penetrating domain, studied in oncology research for selective membrane interaction.
Experimental models examine binding to membrane-associated HDM-2 and the resulting pore formation in cancer cell lines.
PNC-27 combines residues 12-26 of the p53 transactivation domain with the penetratin sequence from the Antennapedia homeodomain. Research has characterized its binding to HDM-2 presented in the plasma membrane of cancer cells, a target reported to be largely absent from the membranes of normal cells.
Structural work describes the peptide adopting an HDM-2-binding conformation, with downstream transmembrane pore formation and necrotic lysis rather than apoptosis. Studies span leukemia, cervical, and pancreatic cancer models.
PNC-27 emerged from research on anticancer peptides derived from the ras-p21 and p53 proteins, in which short functional domains were fused to cell-penetrating sequences.
Subsequent work identified membrane-bound HDM-2 as the selectivity determinant and characterized the membrane-pore mechanism now described as "poptosis".
Research into PNC-27 focuses on selective interaction with membrane-bound HDM-2 and transmembrane pore formation in tumour cells. Frameworks evaluate conformational binding, membrane selectivity, necrotic versus apoptotic cell death, and mitochondrial membrane effects under controlled in vitro conditions.
4 of the 4 areas below are addressed directly by a paper cited on this page.
Membrane-bound HDM-2 targeting models
Addressed on this page by Thadi 2020, Krzesaj 2024, Sarafraz-Yazdi 2010. Each is linked to its source record in the references below, so what was measured — and in what system — can be read rather than taken on trust.
- Thadi, A. et al. (2020) — Targeting Membrane HDM-2 by PNC-27 Induces Necrosis in Leukemia Cells But Not in Normal Hematopoietic Cells
- Krzesaj, P. et al. (2024) — Anti-Cancer Peptide PNC-27 Kills Cancer Cells by Unique Interactions with Plasma Membrane-Bound hdm-2 and with Mitochondrial Membranes Causing Mitochondrial Disruption
- Sarafraz-Yazdi, E. et al. (2010) — Anticancer peptide PNC-27 adopts an HDM-2-binding conformation and kills cancer cells by binding to HDM-2 in their membranes
Cell-penetrating peptide chimera design
Addressed on this page by Sarafraz-Yazdi 2010, Sarafraz-Yazdi 2022, Krzesaj 2024. Each is linked to its source record in the references below, so what was measured — and in what system — can be read rather than taken on trust.
- Sarafraz-Yazdi, E. et al. (2010) — Anticancer peptide PNC-27 adopts an HDM-2-binding conformation and kills cancer cells by binding to HDM-2 in their membranes
- Sarafraz-Yazdi, E. et al. (2022) — PNC-27, a Chimeric p53-Penetratin Peptide Binds to HDM-2 in a p53 Peptide-like Structure, Induces Selective Membrane-Pore Formation and Leads to Cancer Cell Lysis
- Krzesaj, P. et al. (2024) — Anti-Cancer Peptide PNC-27 Kills Cancer Cells by Unique Interactions with Plasma Membrane-Bound hdm-2 and with Mitochondrial Membranes Causing Mitochondrial Disruption
Transmembrane pore formation and necrosis
Addressed on this page by Pincus 2024, Sarafraz-Yazdi 2022, Sarafraz-Yazdi 2010. Each is linked to its source record in the references below, so what was measured — and in what system — can be read rather than taken on trust.
- Pincus, MR. et al. (2024) — Poptosis or Peptide-Induced Transmembrane Pore Formation: A Novel Way to Kill Cancer Cells without Affecting Normal Cells
- Sarafraz-Yazdi, E. et al. (2022) — PNC-27, a Chimeric p53-Penetratin Peptide Binds to HDM-2 in a p53 Peptide-like Structure, Induces Selective Membrane-Pore Formation and Leads to Cancer Cell Lysis
- Sarafraz-Yazdi, E. et al. (2010) — Anticancer peptide PNC-27 adopts an HDM-2-binding conformation and kills cancer cells by binding to HDM-2 in their membranes
Selective tumour-cell cytotoxicity research
Addressed on this page by Sarafraz-Yazdi 2022, Sarafraz-Yazdi 2010, Thadi 2020. Each is linked to its source record in the references below, so what was measured — and in what system — can be read rather than taken on trust.
- Sarafraz-Yazdi, E. et al. (2022) — PNC-27, a Chimeric p53-Penetratin Peptide Binds to HDM-2 in a p53 Peptide-like Structure, Induces Selective Membrane-Pore Formation and Leads to Cancer Cell Lysis
- Sarafraz-Yazdi, E. et al. (2010) — Anticancer peptide PNC-27 adopts an HDM-2-binding conformation and kills cancer cells by binding to HDM-2 in their membranes
- Thadi, A. et al. (2020) — Targeting Membrane HDM-2 by PNC-27 Induces Necrosis in Leukemia Cells But Not in Normal Hematopoietic Cells
The references section of this page cites 5 primary papers published between 2010 and 2024 — a limited but non-trivial record. Every citation is linked to its PubMed or DOI record so it can be read rather than taken on trust, and the summaries above describe what those papers report rather than what the compound is claimed to do.
Research compounds attract claims that outrun their evidence. Below are the ones most often encountered for PNC-27, set against what the papers cited on this page actually report. Where the record is thin or contested, that is stated rather than smoothed over.
PNC-27 is also referred to as PNC, and technically as p53(12-26)-penetratin chimera.
PNC-27 is commonly described online in connection with more energy, better mitochondrial function and slower ageing. In the research literature the same compound is filed under membrane-bound HDM-2 targeting models, cell-penetrating peptide chimera design and transmembrane pore formation and necrosis.
The 5 papers cited on this page, published between 2010 and 2024 describe laboratory and animal work. None reports a controlled trial in humans. Findings in cell culture or in a rodent model describe what happened in that system; they do not establish that the same occurs in humans, and this compound is not approved for human use.
Nothing above is a statement of what this material does. It is a summary of what has been published and what has not. Eppix Labs supplies research materials only and provides no dosing, administration or protocol guidance.
Verification for PNC-27 is per lot, not per product. The current 30mg lot PNC2-CA-26G-30 returned 98.935% purity, 32.14 mg measured, 107.1% of the labelled 30 mg, assayed by Janoshik. Those figures are the laboratory's, published in full rather than reduced to a badge.
Purity is half the number. It states what fraction of the material in the vial is PNC-27; it says nothing about how much material is in the vial, and a short-filled vial can return a purity result that is entirely accurate. The figure that answers the second question is measured mass against expected content — for PNC-27, this lot measured 107.1% of its labelled 30 mg. Both numbers are published for every lot, whichever way they fall.
The lot code printed on the vial matches the code on the certificate for PNC-27. Matching the two is what confirms the unit in hand came from the batch that was tested — a certificate not tied to a lot code proves nothing about any particular unit.
Researchers who buy PNC-27 in the United States through Eppix Labs receive the lot described by the certificate above: the code printed on the vial label is the code on the certificate, and both are searchable on the batch verification page.
- Lyophilized storage
- −20 °C long-term; stable at room temperature in transit
- After reconstitution
- 2–8 °C
- Light
- Protect from UV and direct light
- Freeze-thaw
- Avoid repeated cycles
- Vehicle
- Bacteriostatic water in most published protocols
- Format
- Lyophilized powder
PNC-27 is supplied as lyophilized powder. In the dry state the material is comparatively stable, which is why it ships at ambient temperature without a cold chain; once reconstituted it is a peptide in solution and the handling constraints tighten considerably. At 32 residues it is short enough to be produced by solid-phase synthesis, and the published sequence on this page is what an identity assay is checked against.
Repeated freeze-thaw cycling is the handling error most likely to degrade material of this class, because each cycle concentrates solutes at the ice boundary. Where a protocol calls for the same vial across multiple sessions, the published literature generally describes aliquoting after reconstitution rather than re-freezing the whole volume.
Vials may appear empty on arrival. Lyophilized material collects at the base of the vial and is often not visible until the vial is inspected under direct light.
- 1 × sealed glass vial in the strength selected (30mg / Single Vial, 30mg / 5-Pack, 30mg / 10-Pack available), batch-labelled
- The batch-linked Certificate of Analysis for the exact lot shipped
- Discreet outer packaging with no product names on the exterior
- FedEx, tracked, typically 1–3 business days domestically
- Bacteriostatic water or any other reconstitution vehicle
- Syringes, needles or filters
- Dosing, administration or protocol guidance of any kind
Reconstitution materials are sourced separately. The reconstitution calculator on this site works out concentrations for a given volume, but it is an arithmetic tool for laboratory record-keeping and not a protocol.
No. Eppix Labs products are supplied exclusively for laboratory research. We do not provide dosing, administration, or usage guidance.
Each unit contains the labeled quantity of PNC-27. Independent third-party analysis verifies purity, identity, and net content per batch.
The unit contains only the research compound. Any laboratory materials required for reconstitution or experimental procedures must be sourced separately.
Duration depends entirely on research design, storage conditions, and laboratory protocol.
Anticancer peptide PNC-27 adopts an HDM-2-binding conformation and kills cancer cells by binding to HDM-2 in their membranes
PubMedPNC-27, a Chimeric p53-Penetratin Peptide Binds to HDM-2 in a p53 Peptide-like Structure, Induces Selective Membrane-Pore Formation and Leads to Cancer Cell Lysis
PubMedTargeting Membrane HDM-2 by PNC-27 Induces Necrosis in Leukemia Cells But Not in Normal Hematopoietic Cells
PubMedAnti-Cancer Peptide PNC-27 Kills Cancer Cells by Unique Interactions with Plasma Membrane-Bound hdm-2 and with Mitochondrial Membranes Causing Mitochondrial Disruption
PubMedPoptosis or Peptide-Induced Transmembrane Pore Formation: A Novel Way to Kill Cancer Cells without Affecting Normal Cells
PubMedRelated
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