Humanin For Sale — Research Grade
PX1 Research supplies laboratory-grade Humanin synthesized in state-of-the-art USA facilities for advanced in vitro and preclinical research applications. Every lot undergoes rigorous third-party verification via HPLC and mass spectrometry to guarantee exceptional purity and lot-to-lot consistency.
Quick answer
PX1 Research supplies laboratory-grade Humanin synthesized in state-of-the-art USA facilities for advanced in vitro and preclinical research applications. Every lot undergoes rigorous third-party verification via HPLC and mass spectrometry to guarantee exceptional purity and lot-to-lot consistency.
Key takeaways
- When procurement officers and principal investigators evaluate sources of Humanin for sale, peptide purity, analytical verification, and supply chain integrity represent the paramount criteria.
- Humanin (HN) was the first mitochondrial-derived peptide (MDP) discovered, isolated during functional screening of cDNA libraries derived from post-mortem brain tissue.
- In vitro data indicate that Humanin interacts with two primary receptor complexes: a cell-surface heterotrimeric receptor composed of ciliary neurotrophic factor receptor (CNTFR), WSX-1, and gp130, as well as the formyl peptide receptor-like 1 (FPRL1/FPR2).
- To contextualize Humanin within the broader landscape of mitochondrial bioenergetic modulators, researchers frequently compare its activity against related endogenous and synthetic compounds.
Sourcing High-Purity Humanin for Laboratory Research
When procurement officers and principal investigators evaluate sources of Humanin for sale, peptide purity, analytical verification, and supply chain integrity represent the paramount criteria. Humanin is a unique 24-amino-acid micropeptide encoded within the mitochondrial 16S ribosomal RNA gene. Due to its specific biophysical characteristics and tendency to aggregate if improperly synthesized or stored, acquiring verified research-grade material is essential for reproducible scientific outcomes.
PX1 Research addresses the stringent demands of modern bench science by manufacturing Humanin in domestic, GMP-compliant facilities. Investigators requiring consistent, sequence-verified material for cell culture assays or animal models can rely on our comprehensive analytical documentation. Every batch is subjected to independent ISO 17025 lab verification, confirming structural integrity, sequence fidelity, and low endotoxin levels prior to dispatch.
Biological Structure and Mitochondrial Origin of Humanin
Humanin (HN) was the first mitochondrial-derived peptide (MDP) discovered, isolated during functional screening of cDNA libraries derived from post-mortem brain tissue. The peptide sequence—Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-ID-Asp-Leu-Trp-Asp-Asp-Arg-Cys-Val—encodes a hydrophobic core that plays a crucial role in its structural conformation and receptor binding interactions.
In nature, Humanin is transcribed within the mitochondrion and released into the cytosol or extracellular space. Preclinical studies suggest that Humanin functions as an autocrine, paracrine, and endocrine signaling factor. Researchers studying cellular bioenergetics often utilize our research peptides catalog to explore how micropeptides coordinate nuclear and mitochondrial genome communications during metabolic stress.
Preclinical Mechanisms and Cellular Pathways
In vitro data indicate that Humanin interacts with two primary receptor complexes: a cell-surface heterotrimeric receptor composed of ciliary neurotrophic factor receptor (CNTFR), WSX-1, and gp130, as well as the formyl peptide receptor-like 1 (FPRL1/FPR2). Engagement of these receptors activates downstream intracellular cascades, including the STAT3 (signal transducer and activator of transcription 3) and ERK1/2 pathways.
Furthermore, intracellular Humanin directly binds and sequesters pro-apoptotic Bcl-2 family proteins, such as Bax, Bid, and Bim. By preventing the translocation of Bax to the outer mitochondrial membrane, Humanin inhibits mitochondrial outer membrane permeabilization (MOMP) and subsequent cytochrome c release. Rodent models demonstrate that this mechanism attenuates programmed cell death under conditions of oxidative stress, hypoxia, and excitotoxicity. Researchers investigating metabolic signaling pathways can access full technical specifications in the PX1 research library.
Comparative Analysis: Humanin, MOTS-c, SHLP2, and SS-31
To contextualize Humanin within the broader landscape of mitochondrial bioenergetic modulators, researchers frequently compare its activity against related endogenous and synthetic compounds. While Humanin primary mediates cytoprotective and anti-apoptotic signaling via extracellular receptors and intracellular Bax binding, other mitochondrial signaling molecules exhibit distinct target profiles.
For example, MOTS-c is another mitochondrial-derived peptide encoded in the 12S rRNA region that primarily acts as a metabolic regulator, translocating to the nucleus under metabolic stress to modulate folates and AMPK activity. Similarly, Small Humanin-Like Peptide 2 (SHLP2) shares cytoprotective properties with Humanin but exhibits distinct potencies in insulin sensitization assays. In contrast, the synthetic tetrapeptide SS-31 (Elamipretide) targets cardiolipin on the inner mitochondrial membrane rather than functioning through transcriptionally derived receptor pathways. Evaluating these distinct compounds side-by-side allows research institutions to map specific pathways across cell lines and animal models.
Quality Control: HPLC, Mass Spectrometry, and Endotoxin Verification
Achieving consistent preclinical results requires absolute purity. PX1 Research mandates high-performance liquid chromatography (HPLC) and electrospray ionization mass spectrometry (ESI-MS) testing for every production lot of Humanin. HPLC testing verifies that chemical purity meets or exceeds 98%, ruling out truncated sequences, deletion peptides, and side-chain modified impurities.
In addition to sequence validation, routine endotoxin testing is conducted via the Limulus Amebocyte Lysate (LAL) assay to ensure low endotoxin thresholds (<0.1 EU/mg). This step is critical for cell culture protocols and in vivo studies where bacterial lipopolysaccharide contamination could confound inflammatory marker analyses or cell viability assays. Laboratories can review lot-specific Certificates of Analysis (COAs) directly prior to placing orders.
Reconstitution Protocols and Lyophilized Peptide Handling
Humanin is supplied as a sterile-filtered, lyophilized powder to preserve stability during transit and long-term storage. Due to the hydrophobic nature of its central leucine-rich region, proper reconstitution procedures are necessary to prevent peptide aggregation or precipitation.
For optimal laboratory preparation, lyophilized Humanin should be equilibrated to room temperature before opening the vial. Centrifuging the vial briefly at low speed ensures the powder consolidates at the bottom. The compound should be initially solubilized in sterile, deionized water or a mild buffer solution (such as PBS at pH 7.4). For sensitive cell assays, gentle sonication or brief vortexing may be applied. Avoid vigorous agitation to prevent shear-induced aggregation. Reconstituted stock solutions should be aliquoted and stored at -80°C to minimize freeze-thaw degradation cycles.
In Vitro and In Vivo Research Applications
Preclinical literature documents a wide array of research applications for Humanin. In vitro models utilizing neuronal cell lines (such as PC12 or primary cortical neurons) frequently employ Humanin to evaluate cytoprotection against neurotoxic insults, including amyloid-beta oligomers and glutamate excitotoxicity.
In vascular and metabolic research, animal models have demonstrated Humanin's involvement in endothelial nitric oxide synthase (eNOS) activation, vascular relaxation, and systemic insulin sensitivity. Researchers studying metabolic dysfunction often pair Humanin with other metabolic peptides such as Sermorelin or tissue repair compounds like BPC-157 to evaluate synergistic cross-talk in physiological signaling systems.
PX1 Research Supply Chain: Facilities, Warehousing, and Same-Day Dispatch
Supply chain disruptions can severely compromise trial schedules and ongoing laboratory projects. PX1 Research maintains centralized inventory facilities strategically located in California and Arizona. This dual-hub distribution model ensures seamless order processing and rapid transit across North America.
All orders placed Monday through Friday before 3:00 PM EST are dispatched same-day. Lyophilized peptides are packaged in temperature-controlled, light-shielded containers to maintain bioactivity from our facility to your laboratory bench. This commitment to inventory readiness ensures that academic institutions and biotech organizations receive research materials without costly delays.
Wholesale and Institutional Procurement
For university research departments, contract research organizations (CROs), and industrial biotech firms requiring bulk quantities, PX1 Research provides scalable procurement solutions. Custom vial sizing, batch-reserved inventory, and specialized packaging are available to match institutional research protocols.
Principal investigators and procurement departments can access dedicated account support, tailored volume pricing, and automated compliance documentation through our institutional procurement portal. Contact our technical support team to coordinate large-scale production runs or specialized analytical testing requirements.
Frequently Asked Questions
What is the purity level of Humanin available from PX1 Research?
PX1 Research provides Humanin for sale with verified purity levels exceeding 98%. Each lot undergoes rigorous testing via High-Performance Liquid Chromatography (HPLC) and Mass Spectrometry (MS).
Are Certificates of Analysis (COA) provided with Humanin orders?
Yes. Every single batch of Humanin is accompanied by a lot-specific Certificate of Analysis detailing HPLC purity profiles, mass spec mass verification, and endotoxin assay results from an independent ISO 17025 accredited laboratory.
How should lyophilized Humanin be stored upon receipt?
Lyophilized Humanin powder should be stored at -20°C or -80°C in a dry environment protected from light. Under these conditions, the peptide remains stable for up to 24 months.
What solvent is recommended for reconstituting Humanin for laboratory assays?
Humanin reconstitutes well in sterile water or phosphate-buffered saline (PBS, pH 7.4). Due to its hydrophobic core, gentle vortexing or short sonication may be utilized if needed. Avoid harsh physical agitation.
What are the endotoxin limits for PX1 Research Humanin?
Our standard quality control specifications enforce endotoxin levels strictly below 0.1 EU/mg, verified via standard Limulus Amebocyte Lysate (LAL) testing, making it ideal for sensitive in vitro and in vivo models.
Where does PX1 Research ship Humanin from?
All orders are fulfilled directly from our temperature-controlled warehouses located in California and Arizona. Orders placed before 3:00 PM EST Monday through Friday ship same-day.
Can Humanin be purchased in bulk for high-throughput screening?
Yes. Institutional buyers and CROs can request bulk quantities, custom vial concentrations, or batch reservations through our wholesale account management program.
Is Humanin approved for human therapeutic use or clinical administration?
No. Humanin supplied by PX1 Research is strictly sold as a research compound intended exclusively for laboratory research, in vitro experiments, and preclinical animal studies. It is not for human or veterinary use.
All products are sold strictly for laboratory and research use only. Not for human or veterinary use, diagnosis, treatment or consumption. Statements have not been evaluated by the FDA.