Humanin (HNG)

Description

Disclaimer: This compound is provided strictly for laboratory and scientific research purposes only. It is not approved by the U.S. Food and Drug Administration (FDA) for human or veterinary use,including ingestion, injection, or any form of administration.

Compound Overview

Humanin is a 24-amino acid signaling peptide encoded by an open reading frame within the mitochondrial 16S ribosomal RNA gene. This unique mitochondrial origin distinguishes Humanin from nuclear-encoded peptides and makes it a relevant research tool for investigating organelle-to-nucleus signaling pathways within institutional research frameworks.

Originally characterized in screening studies investigating cellular resistance mechanisms, Humanin has since been studied across multiple research domains including apoptosis signaling, neuronal cell biology, metabolic regulation pathways, and oxidative stress response mechanisms in preclinical model systems.

Humanin is not a SARM, not a hormone analog, and not a dietary supplement. It is not approved by the FDA for human or veterinary use and is intended strictly for institutional laboratory research purposes.

Chemical Properties of the Compound

Institutional Research Compliance Framework

BC9 provides Humanin Peptide specifically for institutional research applications. All purchases must comply with applicable institutional review and animal care framework requirements.

Institutional Review Board (IRB) Considerations

• Any human-subject research involving compound-related protocols requires IRB approval before initiation
• BC9 does not supply Humanin for human research applications under any circumstance
• Institutional research compliance officers should verify protocol approval before procurement

Institutional Animal Care and Use Committee (IACUC) Framework

• Preclinical animal research involving Humanin requires IACUC approval per the Animal Welfare Act (AWA)
• Standard preclinical protocols include controlled dosing, monitoring procedures, and ethical review documentation
• BC9 supplies for IACUC-approved research programs only

Regulatory Documentation Available

• Certificate of Analysis (COA) per production batch
• Safety Data Sheet (SDS) available upon institutional request
• Material handling documentation
• Institutional purchase order documentation support
• Laboratory record-keeping format support
• Batch traceability for research reproducibility

For Research Compliance Officers

BC9 maintains documentation supporting institutional purchasing processes for research compound procurement. Verification documentation is available to research compliance teams as needed for grant management and institutional reporting requirements.

Working Mechanism of Humanin Peptide

Bcl-2 Family Protein Interaction

In preclinical cell culture systems, Humanin has been investigated for its binding interactions with pro-apoptotic Bax protein and related Bcl-2 family members. Research has documented Humanin’s ability to interfere with Bax activation in experimental cell death models, providing a mechanism by which it modulates the intrinsic apoptotic pathway in cell culture systems.

FPRL1 Receptor-Mediated Signaling

Studies in isolated neuronal cell systems have characterized Humanin as a functional ligand for formyl peptide receptor-like 1 (FPRL1), a G protein-coupled receptor. This receptor-mediated mechanism has been documented in preclinical neuronal cultures and represents a distinct signaling pathway from direct intracellular protein binding.

IGFBP-3 Complex Formation

In cell-free binding assays and isolated cell preparations, Humanin has been documented to form a functional complex with insulin-like growth factor binding protein-3 (IGFBP-3). This interaction has been characterized in preclinical research models and is studied for its role in cellular signaling pathway modulation and apoptosis regulation.

Insulin Signaling Pathway Modulation

In preclinical metabolic research models, particularly rodent studies, Humanin has been investigated for its role in insulin signaling pathway regulation. Data suggest the peptide may modulate peripheral insulin sensitivity through mechanisms involving hypothalamic STAT3 signaling pathways in animal model systems.

Oxidative Stress Response Pathways

Research in endothelial and vascular cell culture systems has documented Humanin’s interaction with oxidative stress response pathways. In oxidized LDL exposure models, Humanin has been associated with modulation of cellular stress markers and preservation of cellular integrity in experimental conditions.

Research Findings and Research Applications

Preclinical investigations have examined Humanin peptide in relation to multiple research domains:

In controlled laboratory environments, Humanin has been investigated for mitochondrial-derived peptide signaling kinetics and structure-activity relationship (SAR) studies, Bcl-2 family protein interaction and apoptosis pathway modulation research, and as a reference compound in cellular stress response assays using preclinical oxidative stress models.

Research has further examined Humanin’s role in FPRL1 and FPRL2 receptor binding characterization, IGFBP-3 complex formation and peptide-protein interaction studies, insulin signaling pathway investigation in metabolic research frameworks, and comparative mitochondrial peptide pharmacology studies contrasting Humanin’s cytoprotective receptor binding profile against other mitochondria-associated peptides such as MOTS-c and SHLPs.

Note: These findings are based on preclinical research conducted in animal models and cell culture systems. Results are not consistent across all experimental conditions, and data remains limited without validation in human clinical research settings.

Risk & Handling

PPE Requirements: The use of appropriate personal protective equipment is essential when conducting research with Humanin. Required PPE includes nitrile gloves, lab coat, and eye protection at minimum.

Laboratory Environment: Handling should occur within controlled laboratory environments specifically designed for research activities, with appropriate ventilation and biosafety measures.

Exposure Precautions: Do not inhale, ingest, or make direct skin contact with the compound. Avoid inhalation of lyophilized powder during weighing or reconstitution procedures.

Toxicological Profile: The toxicological profile is not fully established for the research-grade formulation supplied here. Exposure risks remain uncertain due to limited long-term safety data. No human safety data has been established for this research-grade formulation.

Storage and Stability: Improper storage conditions, including exposure to heat, light, or moisture, may result in compound degradation and compromised sample integrity. The vial seal should remain intact until use. Avoid repeated freeze-thaw cycles.

For queries, complaints, or support, please contact support@bc9.co

Frequently Asked Questions

What makes Humanin a mitochondria-derived peptide in research contexts?

16S ribosomal RNA gene, making it one of the first identified mitochondrial-genome-encoded signaling peptides. This mitochondrial origin distinguishes it from nuclear-encoded peptides and provides researchers with a useful tool for investigating organelle-to-nucleus signaling pathways in preclinical research models.

Is Humanin Peptide approved for human use?

No. Humanin Peptide is not approved by the FDA for human or veterinary use. The research-grade formulation supplied by BC9 is intended strictly for institutional laboratory research purposes only.

What is the recommended vial format for Humanin Peptide from BC9?

Humanin Peptide is supplied as a lyophilized powder in a sterile, sealed vial with a flip-top aluminium crimp cap. This format maintains peptide integrity under recommended cold storage conditions and meets standards for research-grade lyophilized peptides used in institutional research applications.

What documentation is available for institutional research purchases?

BC9 provides Certificate of Analysis (COA) per batch, Safety Data Sheet (SDS) upon request, batch traceability documentation, and institutional purchase order support. Research compliance officers can request additional documentation as needed for grant management or institutional reporting purposes.

How does Humanin compare to other mitochondrial-derived peptides?

Humanin is distinguished from other mitochondrial-derived peptides (MDPs) such as MOTS-c and the SHLPs by its 24-amino acid structure, its specific encoding from the 16S rRNA gene, and its documented binding interactions with Bcl-2 family proteins, FPRL1 receptors, and IGFBP-3. These mechanism distinctions position Humanin as a unique research tool within the broader MDP research category.

References

1. Hashimoto, Y., Niikura, T., Tajima, H., et al. (2001). A rescue factor abolishing neuronal cell death by a wide spectrum of familial Alzheimer’s disease genes and Aβ. Proceedings of the National Academy of Sciences, 98(11), 6336–6341. https://doi.org/10.1073/pnas.191380498
2. Guo, B., Zhai, D., Cabezas, E., Welsh, K., Nouraini, S., Satterthwait, A.C., & Reed, J.C. (2003). Humanin peptide suppresses apoptosis by interfering with Bax activation. Nature, 423(6938), 456–461. https://doi.org/10.1038/nature01627 
3. Ikonen, M., Liu, B., Hashimoto, Y., et al. (2003). Interaction between the Alzheimer’s survival peptide humanin and insulin-like growth factor-binding protein 3 regulates cell survival and apoptosis. Proceedings of the National Academy of Sciences, 100(22), 13042–13047. https://pmc.ncbi.nlm.nih.gov/articles/PMC240741/ 
4. Ying, G., Iribarren, P., Zhou, Y., et al. (2004). Humanin, a newly identified neuroprotective factor, uses the G protein-coupled formylpeptide receptor-like-1 as a functional receptor. Journal of Immunology, 172(11), 7078–7085. https://doi.org/10.4049/jimmunol.172.11.7078 
5. Muzumdar, R.H., Huffman, D.M., Atzmon, G., et al. (2009). Humanin: a novel central regulator of peripheral insulin action. PLoS ONE, 4(7), e6334. https://doi.org/10.1371/journal.pone.0006334 
6. Bachar, A.R., Scheffer, L., Schroeder, A.S., et al. (2010). Humanin is expressed in human vascular walls and has a cytoprotective effect against oxidized LDL-induced oxidative stress. Cardiovascular Research, 88(2), 360–366. https://doi.org/10.1093/cvr/cvq191 
7. Yen, K., Lee, C., Mehta, H., & Cohen, P. (2013). The emerging role of the mitochondrial-derived peptide humanin in stress resistance. Journal of Molecular Endocrinology, 50(1), R11–R19. https://pubmed.ncbi.nlm.nih.gov/23239898/

This content is presented exclusively for educational purposes and should not be construed as medical advice. THE MATERIALS REFERENCED HEREIN ARE EXCLUSIVELY INTENDED FOR LABORATORY AND RESEARCH USE.

Any clinical research initiatives must be conducted under the guidance of the relevant Institutional Review Board (IRB). Similarly, preclinical research involving animals must comply with the directives of the Institutional Animal Care and Use Committee (IACUC), adhering to the standards delineated by the Animal Welfare Act (AWA).

Our informational content is meticulously designed for research-oriented insights and is not a substitute for individual analysis and verification from credible sources before any purchasing decisions are made.

Upon finalizing your order and payment, you explicitly acknowledge and agree to adhere to our Terms and Conditions. Customer satisfaction stands as our paramount concern. If you are dissatisfied with the product received, kindly contact us at support@bc9.co

IMPORTANT NOTICE: All products showcased on our platform are EXCLUSIVELY INTENDED FOR LABORATORY AND RESEARCH APPLICATIONS. They are expressly not intended for veterinary or human utilization.