Buy Humanin

Sourcing High-Purity Humanin for Laboratory Research

To buy Humanin for laboratory research, qualified investigators require authenticated, USA-manufactured peptides verified via RP-HPLC and mass spectrometry. Humanin is a 24-amino-acid mitochondrial-derived peptide studied in cellular cytoprotection, neurobiology, and metabolic signaling models. PX1 Research provides research-grade Humanin (>98% purity) with lot-specific COAs, endotoxin analysis, and same-day dispatch for institutional research facilities.

Humanin represents a distinct class of signaling molecules encoded within the 16S ribosomal RNA gene of the mitochondrial genome. When purchasing research-grade materials, researchers must ensure that suppliers maintain rigorous quality controls, as secondary structures and hydrophobic regions in mitochondrial-derived peptides make synthesis uniquely challenging. Substandard synthesis can lead to truncated sequences or aggregation artifacts that compromise assay fidelity.

When you select PX1 Research to buy Humanin, your laboratory receives material produced under strict GMP-compliant guidelines within ISO 17025 accredited facilities. Every lot is provided exclusively for in vitro and laboratory research applications, supported by transparent analytical data to verify sequence integrity and batch consistency.

Molecular Structure and Synthesis of Mitochondrial-Derived Peptides

Humanin (HN) is characterized by its 24-amino-acid sequence: Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala. It possesses a hydrophobic core dominated by leucine residues, which confers unique physical properties and dictates its solubility and receptor interaction profiles. In native biological systems, Humanin acts as an endogenous cytoprotective factor generated during cellular stress.

Solid-phase peptide synthesis (SPPS) of Humanin demands precise optimization to prevent racemization and incomplete coupling, particularly across the leucine-rich central domain. PX1 Research utilizes advanced automated SPPS technologies followed by multi-step purification protocols to eliminate hydrophobic side-products and deletion sequences.

The resulting purified lyophilized powder maintains precise structural fidelity. Investigating such specialized mitochondrial signaling factors allows researchers in cell biology and bioenergetics to explore complex intercellular communication networks, expanding upon findings established with other research peptides in mitochondrial genomics.

Mechanism of Action: Receptors and Cytoprotective Pathways

Preclinical literature demonstrates that Humanin mediates cytoprotection through both extracellular receptor engagement and intracellular protein-protein interactions. Extracellularly, Humanin acts as a ligand for a heterotrimeric receptor complex consisting of ciliary neurotrophic factor receptor (CNTFR), glycoprotein 130 (gp130), and interleukin-27 receptor subunit alpha (WSX-1). Additionally, it binds the G-protein coupled receptor formyl peptide receptor-like 1 (FPRL1 / FPR2).

Upon receptor binding, in vitro assays show that Humanin initiates intracellular signaling cascades, primarily driving the phosphorylation of Signal Transducer and Activator of Transcription 3 (STAT3) and Extracellular Signal-Regulated Kinase (ERK1/2). STAT3 activation upregulated downstream anti-apoptotic targets, helping preserve mitochondrial membrane potential under chemically induced oxidative stress conditions.

Intracellularly, physical binding assays indicate that Humanin interacts directly with pro-apoptotic proteins, including Bax, Bid, and Bim. By sequestering these proteins in the cytosol, Humanin prevents their translocation to the outer mitochondrial membrane, thereby inhibiting cytochrome c release and caspase activation. Investigators interested in these cell survival pathways often evaluate Humanin alongside mitochondrial research compounds to map overlapping survival cascades.

Preclinical Literature and Metabolic Research Findings

In vitro data indicate that Humanin exerts significant anti-inflammatory and cytoprotective effects across diverse cell lineages. In primary neuronal culture models, exposure to synthetic Humanin attenuated neurotoxicity induced by amyloid-beta oligomers, excitotoxic glutamate levels, and transcriptional stress. These findings have positioned Humanin as a primary molecular probe in neurodegenerative disease models.

Rodent models investigating metabolic regulation show that central or peripheral administration of Humanin analogues modulates systemic insulin sensitivity. Experimental data suggest that Humanin action in the hypothalamus enhances hepatic insulin sensitivity via STAT3-dependent pathways. Furthermore, animal studies in cardiovascular models demonstrate reduced myocardial infarct size and decreased vascular endothelial apoptosis following ischemia-reperfusion injury protocols.

These preclinical observations underscore the broad utility of Humanin as a laboratory tool for studying metabolic homeostasis, microvascular integrity, and cellular stress resistance. Detailed analytical profiles for research reagents used in these models are available through the PX1 Research catalog.

Comparative Analysis: Humanin, MOTS-c, and SHLP2

Humanin belongs to the broader family of mitochondrial-derived peptides (MDPs), which also includes MOTS-c and the Small Humanin-Like Peptides (SHLPs). While all MDPs originate from mitochondrial DNA, their primary structures, receptor targets, and physiological pathways differ significantly in experimental models.

For instance, MOTS-c is a 16-amino-acid peptide encoded within the 12S rRNA gene that primarily targets skeletal muscle and metabolic tissue via activation of the AMPK pathway and nuclear translocation under metabolic stress. In contrast, SHLP2 is a 26-amino-acid peptide that exhibits chaperone-like properties and enhances mitochondrial bioenergetics similar to Humanin, but operates through distinct binding kinetics and receptor subtypes. Comparing these peptides within identical cell culture lines provides valuable insights into mitochondrial-nuclear signaling cross-talk.

Laboratory Reconstitution and Storage Handling Protocols

Proper reconstitution and handling protocols are critical to maintaining the structural stability and bioactivity of Humanin in laboratory experiments. The lyophilized peptide is sensitive to moisture, temperature fluctuations, and pH extremes.

Reconstitution protocols should be conducted under sterile laminar flow hoods using cold, sterile solvents. While Humanin displays moderate solubility in standard aqueous buffers like Phosphate-Buffered Saline (PBS, pH 7.4), initial solubilization in a minimal volume of sterile water or dilute acetic acid (0.1%) may be required if high-concentration stock solutions are desired, followed by dilution into the final assay medium.

Lyophilized Humanin should be stored at -20°C or -80°C upon receipt, protected from light and desiccation. Reconstituted stock solutions should be aliquoted into single-use polypropylene microcentrifuge tubes to prevent degradation caused by repeated freeze-thaw cycles. Stock aliquots stored at -80°C typically remain stable for research use over extended experimental windows.

Analytical Quality Verification: RP-HPLC, Mass Spectrometry, and Endotoxin Testing

Analytical rigor is essential when sourcing peptides for quantitative laboratory assays. PX1 Research enforces a rigorous verification pipeline for every production lot of Humanin. Purity is determined using Reversed-Phase High-Performance Liquid Chromatography (RP-HPLC) with UV detection, ensuring that the target peptide peak accounts for greater than 98% of the total integrated area.

Mass identity is verified through Electrospray Ionization Mass Spectrometry (ESI-MS) or MALDI-TOF analysis, confirming that the observed molecular weight precisely matches the theoretical mass of 2687.2 Da. This step eliminates the risk of misidentified sequences, truncated impurities, or incomplete deprotection artifacts.

Crucially for cell culture and immunological assays, PX1 Research performs quantitative endotoxin testing using the chromogenic Limulus Amebocyte Lysate (LAL) assay. Ensuring endotoxin levels remain below 0.1 EU/mg prevents non-specific inflammatory signaling in delicate in vitro models. Researchers can review these parameters in detail via our quality assurance hub.

USA Manufacturing and Lot-Specific Quality Assurance

PX1 Research manufactures all research peptides in modern, GMP-compliant facilities located within the United States. Domestic synthesis allows for strict adherence to quality management systems, eliminating the uncertainties associated with unverified foreign imports.

Every batch of Humanin is assigned a unique lot number that links directly to its complete analytical dossier. Qualified institutional buyers can access downloadable Certificate of Analysis (COA) documents detailing RP-HPLC chromatograms, mass spectra, residual solvent analysis, and endotoxin levels for their specific lot.

This level of lot traceability ensures that academic institutions, biotechnology firms, and contract research organizations (CROs) maintain full experimental compliance. Principal investigators managing high-throughput screens or long-term studies can also utilize the PX1 wholesale portal to secure dedicated single-lot reserves.

Fulfilling Institutional Procurement and Research Standards

PX1 Research streamlines procurement for institutional purchasing agents, laboratory managers, and university departments. Orders ship directly from our centralized distribution facilities in California and Arizona, offering same-day dispatch for orders placed before standard cutoff times Monday through Friday.

By maintaining dedicated inventory reserves within US borders, PX1 Research eliminates supply chain delays and customs risks. Whether your laboratory requires single vials for exploratory benchtop assays or bulk quantities for systematic screening programs, PX1 Research provides the reliable supply and documentation required by modern scientific standards.