📄 Certificate of Analysis available on request
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Humanin is a 24-amino-acid peptide of the mitochondrial-derived peptide class, encoded within the mitochondrial 16S rRNA gene region. It is supplied here as a synthetic research compound.
In the published preclinical literature, Humanin has been characterised at the molecular and cellular level for its interaction with a cell-surface receptor complex and with intracellular protein partners, and in cell-based assays of apoptotic-pathway and mitochondrial signalling chemistry. It is supplied as a research compound and is not intended for human or veterinary use.
Humanin has been characterised in preclinical laboratory models. The primary studies below, in cell-based and cell-free biochemical systems, examined molecular and cellular endpoints, with the work centred on the peptide’s direct protein binding and its interaction with cell-surface receptors. The literature is preclinical; it describes the compound, not any outcome in humans.
In vitro
Humanin peptide suppresses apoptosis by interfering with Bax activation
In cultured cells and cell-free assays, the study measured direct binding of the peptide to the Bax protein and assayed Bax conformational change and its movement to the mitochondrial fraction as molecular endpoints.
Read the study ↗
In vitro
N-Formylated humanin activates both formyl peptide receptor-like 1 and 2
In CHO cells engineered to express FPRL1 or FPRL2, the study assayed receptor engagement by radioligand binding and by the change in forskolin-induced cAMP as cellular signalling endpoints.
Read the study ↗
Full documentation, on the record. A Certificate of Analysis and a Safety Data Sheet are available on request for every batch.
Links open the original study on PubMed. For research and educational purposes, descriptive of the published preclinical literature, not therapeutic claims about any ai-peptides product.
