FOXO4-DRI: research reference

Keep source limits and editorial status visible. A proposed mechanism should not be presented as a confirmed property in every context.

According to structural literature, FOXO4-DRI binds to the TAD2 region of p53; both the FOXO4-derived region and the cell-penetrating segment participate in the interaction. These findings describe the experimental construct.

The purity value is a product-label specification, not an assay result. A batch result can only be asserted from that batch’s certificate.

These names help identify the catalog entry. A descriptive label is not evidence of efficacy, and structural identity still requires appropriate documentation.

D-retro-inverso peptide

Reconstitution: Laboratory procedure: allow the closed vial to reach room temperature, disinfect the septum and slowly transfer the diluent against the inner wall of the vial. Do not shake; gently swirl the vial until fully dissolved. Record the volume, diluent and date in the batch log.

Storage: Sealed vial of lyophilized material: store at −20 °C, protected from light and moisture. Avoid repeated freeze-thaw cycles of reconstituted material; aliquot when the experimental design permits.

Personal protective equipment: Handle in a clean work area with a lab coat, nitrile gloves and eye protection. Dispose of vials, tips and sharps according to the laboratory waste procedure.

FOXO4-DRI is a synthetic retro-inverso peptide, distinct from full-length FOXO4 protein. The foundational 2017 study examined it alongside an L-form version and additional controls. Configuration is part of experimental identity; sharing FOXO4 in a name is insufficient.

The construct includes a FOXO4-derived region and a cell-penetrating segment. Later structural analysis attributed binding participation to both. Describing it only as a FOXO4 fragment omits a relevant part of the design. Sources: PMID 28340339; PMID 40593617.

A 2025 study used nuclear magnetic resonance to characterize p53 complexes with FOXO4 and FOXO4-DRI. It describes peptide binding at the TAD2 region of p53’s transactivation domain, forming a transiently folded complex.

The same work found greater affinity when p53 was phosphorylated. Interaction therefore depends on a molecular condition beyond the proteins’ names. Structural experiments refine binding identity without establishing responses in every cell type. Sources: PMID 40593617.

The 2017 study associated disruption of FOXO4–p53 interaction with p53 movement out of the nucleus and apoptosis in senescent cells. Comparisons included senescent fibroblasts and cellular controls, with experiments on p53 and caspase involvement.

It also examined accelerated-aging mice, naturally aged mice and a doxorubicin-associated damage model, with activity, fur and renal measurements. These are defined-model outcomes, not a universal measure of aging or characterization of a commercial vial. Sources: PMID 28340339.

The 2021 paper examined in vitro-expanded human-donor chondrocytes with different expansion histories. FOXO4-DRI was associated with fewer cells and reduced senescence indicators in the more-expanded population, without a significant cell-number change in the less-expanded control.

Subsequent aggregate culture did not show increased cartilage-forming capacity. Differences did appear in senescence-associated secreted factors in vitro. Changing culture composition and improving tissue function are separate outcomes. Sources: PMID 33996787.

This preparation declares FOXO4-DRI as one ingredient. Multiple segments within one experimental peptide construct do not make it a commercial blend of independent ingredients.

Full sequence, configuration and incorporated segments matter for comparison with literature. The papers do not certify those attributes in a catalog batch. Retro-inverso naming alone cannot establish product half-life, and observed selectivity cannot be extended to every cell population. Sources: PMID 40593617; PMID 33996787.