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(Tetracosapeptide, 24 amino acids)

Brief Summary

Humanin is a synthetic mitochondrial-derived peptide studied in laboratory settings for its relationship with mitochondrial signalling, cellular stress responses and apoptosis-associated pathways. The peptide contains 24 amino acids and is associated with a short open reading frame located within the mitochondrial 16S ribosomal RNA region. Research has focused particularly on its interactions with cellular stress proteins, mitochondrial membrane processes and signalling systems connected with programmed cell death. Humanin has also been examined in neural, metabolic and cellular ageing research models involving oxidative stress, glucose-associated signalling and mitochondrial communication. Within scientific research catalogues, Humanin is valued for in vitro and preclinical investigation involving mitochondrial biology, cellular survival pathways, stress-response signalling and mitochondria-derived peptide activity. Its defined 24-amino-acid sequence supports structured laboratory study, analytical characterisation and reproducible peptide research within professional scientific environments.

Product Overview

Humanin is a laboratory-grade synthetic peptide developed for controlled research into mitochondrial communication, cellular stress regulation and apoptosis-associated signalling. Its amino-acid sequence contains a central leucine-rich region and a cysteine residue at position eight, both of which contribute to its structural and molecular characteristics. Humanin has been examined for its interaction with apoptosis-associated proteins, including Bax, as well as extracellular receptor complexes involving gp130, WSX-1 and the ciliary neurotrophic factor receptor. These molecular interactions allow researchers to investigate both intracellular and extracellular peptide-signalling mechanisms. Humanin is also relevant to comparative studies involving other mitochondrial-derived peptides, including MOTS-c, and mitochondrial-targeted research compounds such as SS-31. Its defined composition and reproducible molecular characteristics support controlled investigation into mitochondrial signalling, oxidative stress responses, cellular communication and age-associated pathway activity.

Scientific Background

From a molecular science perspective, Humanin is studied as a mitochondria-derived peptide involved in communication between mitochondrial activity and wider cellular signalling networks. Experimental research has examined its interaction with Bax, a protein associated with mitochondrial membrane regulation and programmed cell-death signalling. Humanin has also been investigated in relation to extracellular receptor complexes that can activate JAK and STAT-associated intracellular pathways. These different interaction mechanisms allow researchers to examine how one mitochondrial-derived sequence may influence multiple cellular signalling systems. Additional laboratory studies have investigated Humanin in neural cell models, oxidative stress assays, mitochondrial membrane studies and metabolic signalling experiments. Research has also examined its relationship with insulin-associated pathways, inflammatory markers and cellular ageing processes. Humanin therefore provides a useful molecular tool for investigating mitochondrial communication, peptide-protein interactions and the relationship between cellular stress signals and regulated survival pathways.

Research Applications

Humanin is applied in laboratory research across mitochondrial science, molecular biology, neuroactive pathway investigation and cellular bioregulation. Researchers use the peptide to examine mitochondrial stress signalling, Bax-associated pathways, apoptosis regulation, oxidative stress markers and cellular communication under controlled experimental conditions. Additional research applications include neural cell-response studies, mitochondrial membrane analysis, glucose-associated signalling, inflammatory marker evaluation and cellular ageing models. Humanin may also be used to investigate extracellular receptor activity, JAK and STAT-associated pathways and interactions between mitochondria-derived peptides and intracellular proteins. Its 24-residue structure supports research into peptide conformation, sequence-specific signalling, molecular recognition and structure-activity relationships. These applications contribute to a broader understanding of mitochondrial-derived peptide biology and how compact mitochondrial sequences may influence neural, metabolic and cellular stress pathways. Humanin is supplied as a research compound for analytical, in vitro and controlled preclinical investigation only.

Technical Specifications

Contents: 10mg Humanin
Form: Lyophilised powder
Purity: >99% (HPLC Verified)
Molecular Formula: C₁₁₉H₂₀₄N₃₄O₃₂S₂
Molecular Weight: 2687.3 g/mol
Sequence: Methionine–Alanine–Proline–Arginine–Glycine–Phenylalanine–Serine–Cysteine–Leucine–Leucine–Leucine–Leucine–Threonine–Serine–Glutamic Acid–Isoleucine–Aspartic Acid–Leucine–Proline–Valine–Lysine–Arginine–Arginine–Alanine
Peptide Length: 24 amino acids
pH Range: 6.5-7.5
Storage: Store between 1°C and 5°C 

Note: Reconstitute with Bacteriostatic Water

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Disclaimer

For research purposes only. Not for human consumption