Buy Dermorphin
PX1 Research provides researchers with high-purity, USA-manufactured dermorphin for in vitro assays and preclinical laboratory investigation. Every lot undergoes rigorous third-party testing via RP-HPLC and mass spectrometry to guarantee analytical consistency, structural integrity, and verified purity.
Quick answer
PX1 Research provides researchers with high-purity, USA-manufactured dermorphin for in vitro assays and preclinical laboratory investigation. Every lot undergoes rigorous third-party testing via RP-HPLC and mass spectrometry to guarantee analytical consistency, structural integrity, and verified purity.
Key takeaways
- Qualified institutions seeking to buy dermorphin for laboratory research require analytical precision, complete sequence confirmation, and lot-specific purity verification.
- The primary sequence of dermorphin is defined as Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2, with a molecular formula of C40H50N8O10 and a formula weight of 802.9 g/mol.
- Preclinical studies suggest that dermorphin operates as a potent and highly selective agonist for the mu-opioid receptor (MOR).
- In vitro data indicate that dermorphin exhibits remarkable potency in isolated tissue models, such as guinea pig ileum (GPI) and mouse vas deferens (MVD) preparations.
Direct Sourcing & Overview: Buying Research-Grade Dermorphin
Qualified institutions seeking to buy dermorphin for laboratory research require analytical precision, complete sequence confirmation, and lot-specific purity verification. Dermorphin is a naturally occurring heptapeptide (H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2) originally isolated from the skin of South American frogs belonging to the genus Phyllomedusa. It is recognized in chemical biology for containing a D-amino acid residue—specifically D-alanine at position 2—which is an unusual structural post-translational modification in eukaryotic peptides.
Supplied strictly as a research compound for in vitro assays and preclinical laboratory models, dermorphin serves as a benchmark tool for studying mu-opioid receptor kinetics and peptide stability. When ordering from PX1 Research, laboratory investigators receive fully characterized, high-purity material manufactured in GMP-compliant, USA-based facilities.
Molecular Structure and Biochemical Profile of Dermorphin
The primary sequence of dermorphin is defined as Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2, with a molecular formula of C40H50N8O10 and a formula weight of 802.9 g/mol. The incorporation of D-alanine instead of L-alanine at the second position imparts exceptional conformational stability against enzymatic cleavage by native proteases, carboxypeptidases, and aminopeptidases.
In structural biology experiments, the N-terminal tetrapeptide sequence (Tyr-D-Ala-Phe-Gly) functions as the core pharmacophore responsible for receptor activation. Meanwhile, the C-terminal tripeptide fragment (Tyr-Pro-Ser-NH2) stabilizes the spatial orientation needed for selective binding. Research teams investigating structural modifications and peptidomimetics can access comparative datasets through our research library hub.
Receptor Binding Affinity and Mechanism of Action
Preclinical studies suggest that dermorphin operates as a potent and highly selective agonist for the mu-opioid receptor (MOR). In radioligand binding assays using brain membrane homogenates and recombinant cell lines expressing human opioid receptors, dermorphin demonstrates low nanomolar binding affinity (Ki values typically under 1.0 nM) for MOR, while displaying substantially lower affinity for delta-opioid (DOR) and kappa-opioid (KOR) subtypes.
Upon binding the extracellular pocket of the mu-opioid receptor, in vitro assays indicate that dermorphin triggers G-protein activation, leading to the inhibition of adenylyl cyclase activity and modulation of voltage-gated calcium channels. Investigating teams evaluating downstream signaling pathways can select target compounds across our full catalog of all peptides to establish appropriate negative and positive controls.
Preclinical Literature Review: In Vitro and Animal Studies
In vitro data indicate that dermorphin exhibits remarkable potency in isolated tissue models, such as guinea pig ileum (GPI) and mouse vas deferens (MVD) preparations. The peptide suppresses electrically evoked contractions at picomolar to nanomolar concentrations, primarily driven by its high selectivity for pre-junctional mu-opioid receptors.
In rodent models, animal studies have evaluated central and peripheral administration of dermorphin to investigate antinociceptive signaling mechanisms. Investigators have observed that its central potency in thermal and mechanical pain models significantly exceeds that of endogenous mammalian opioid peptides and conventional alkaloid ligands, largely due to its resistance to enzymatic degradation in vivo.
Comparative Analysis: Dermorphin vs. Related Opioid Peptides
When designing comparative binding or signaling panels, researchers frequently evaluate dermorphin alongside related opioid peptides. While dermorphin serves as a gold standard for mu-opioid selectivity, deltorphin represents an ultra-selective delta-opioid receptor agonist isolated from the same amphibian origin. Synthetic analog probes such as DAMGO provide a synthetic benchmark for mu-receptor binding studies, whereas native mammalian ligands like endomorphin 1 display distinctly different enzymatic clearance rates in tissue media.
Establishing side-by-side pharmacological profiles across these diverse ligands allows investigators to map subtle differences in receptor conformational changes and arrestin recruitment. For broad screening initiatives, laboratories can request bulk supply parameters via our wholesale laboratory account program.
Analytical Quality Control: RP-HPLC, Mass Spectrometry, and Endotoxin Testing
To ensure reproducible experimental outcomes, buying dermorphin requires absolute verification of chemical purity and identity. PX1 Research subjects every synthesis lot to rigorous analytical evaluation at an independent, ISO 17025 accredited laboratory.
Purity is verified using Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC), ensuring a baseline chemical purity of equal to or greater than 98%. Electrospray Ionization Mass Spectrometry (ESI-MS) confirms the correct molecular mass and checks for unreacted synthesis intermediates. Additionally, all lots undergo chromogenic Limulus Amebocyte Lysate (LAL) testing to ensure endotoxin levels remain below 0.01 EU/mg, protecting cell cultures from inflammatory artifact responses.
Laboratory Reconstitution Protocols and Solvent Compatibility
Dermorphin is supplied as a lyophilized (freeze-dried) powder to maximize shelf life. For laboratory reconstitution, researchers should dissolve the peptide in sterile, deionized laboratory-grade water or sterile phosphate-buffered saline (PBS, pH 7.4). Gentle vortexing or mild sonication may be utilized to achieve complete dissolution.
If preparing concentrated stock solutions for subsequent dilution into bioassay media, a small volume of sterile 0.1% acetic acid or dimethyl sulfoxide (DMSO) may be used as an initial solvent before adding aqueous buffer. Detailed protocols regarding concentration calculations and solubilization strategies are documented in our peptide solubility and reconstitution guide.
Storage Conditions, Shelf Life, and Handling Instructions
Lyophilized dermorphin should be stored at -20°C or -80°C upon receipt in a desiccated environment protected from light. Under these conditions, the lyophilized peptide remains stable for up to 24 months without significant degradation.
Once reconstituted into aqueous solution, aliquot the peptide into single-use working volumes to minimize repeated freeze-thaw cycles, which can cause physical degradation or peptide aggregation. Reconstituted aliquots stored at -20°C or colder remain viable for preclinical assays for up to 3 to 6 months. Always handle the vial using aseptic technique inside a certified laminar flow hood.
Supplier Evaluation: What Labs Must Require Prior to Purchase
When purchasing specialized heptapeptides for academic or industrial research, principal investigators must carefully screen suppliers for stringent manufacturing standards. Low-quality sources often contain TFA counter-ion contamination, truncated sequences, or high endotoxin burdens that distort in vitro binding data.
PX1 Research differentiates itself by providing fully transparent documentation with every order. All peptides are USA-manufactured in state-of-the-art facilities, accompanied by lot-specific Certificates of Analysis (COAs) accessible online, and dispatched with rapid same-day shipping (Monday through Friday) from logistics centers in California and Arizona.
Summary of Research Applications for Institutional Investigators
Dermorphin remains a key reference tool for biophysical research, structural biology, and receptor pharmacology. Its unique biochemical structure allows researchers to investigate the dynamics of G-protein coupled receptor (GPCR) activation, ligand-receptor binding kinetics, and the role of D-amino acids in conferring enzymatic protection.
By sourcing verified reference materials from PX1 Research, laboratory teams ensure that their preclinical experiments are grounded in chemical purity, batch consistency, and rigorous analytical quality control.
Frequently Asked Questions
What is dermorphin used for in research?
Dermorphin is a research-grade heptapeptide used in laboratory settings to investigate mu-opioid receptor kinetics, signal transduction pathways, and structural modifications involving D-amino acid stability.
Where can laboratories buy dermorphin with verified purity?
Research institutions can buy high-purity dermorphin directly from PX1 Research. Every lot is manufactured in the USA and supplied with independent HPLC, MS, and endotoxin Certificates of Analysis.
What is the molecular sequence and weight of dermorphin?
Dermorphin has the amino acid sequence H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2 and a molecular weight of 802.9 g/mol.
Why is the presence of D-alanine in dermorphin significant?
The D-alanine residue at position 2 confers resistance to cleavage by native peptidases, allowing the peptide to demonstrate enhanced enzymatic stability during in vitro and preclinical assays.
How should lyophilized dermorphin be stored upon delivery?
Lyophilized dermorphin should be stored at -20°C or -80°C in a dry, dark place. Upon reconstitution, it should be aliquoted and kept frozen to avoid freeze-thaw degradation.
What solvent is recommended for reconstituting dermorphin?
Dermorphin easily dissolves in sterile laboratory-grade water or phosphate-buffered saline (PBS, pH 7.4). For highly concentrated stock solutions, a minimal amount of 0.1% acetic acid or DMSO can be used.
What are the endotoxin limits for PX1 Research dermorphin?
PX1 Research verifies that endotoxin levels in dermorphin lots are tested via LAL chromogenic assay to ensure levels remain below 0.01 EU/mg.
How does dermorphin differ from deltorphin in binding assays?
Dermorphin is highly selective for the mu-opioid receptor (MOR), whereas deltorphin is highly selective for the delta-opioid receptor (DOR), making them complementary control tools in receptor binding panels.
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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.