High-purity research peptides synthesized for scientific investigation. Each compound is rigorously tested and intended exclusively for laboratory and research applications.
RIAN Peptides offers a curated selection of high-purity research compounds. Each peptide is independently verified for sequence accuracy, purity, and stability prior to distribution.
Body Protection Compound derived from a gastric protein. Studied for its stability in aqueous environments and interaction with growth factor signaling pathways in preclinical models.
Synthetic analogue of the naturally occurring Thymosin Beta-4 protein. Investigated in research contexts for actin-binding properties and cellular migration studies.
Pentapeptide GH secretagogue with high receptor selectivity in vitro. Commonly referenced in GH axis research due to its minimal effect on cortisol and prolactin pathways in animal models.
Synthetic GHRH analogue engineered for extended half-life through maleimido-propionic acid modification. Used in laboratory settings for sustained GH axis activation studies.
29-amino acid fragment corresponding to the first 29 residues of endogenous GHRH. Extensively used as a research standard in pituitary cell studies and GH secretion assays.
Cyclic heptapeptide melanocortin receptor agonist derived from alpha-MSH. Utilized in CNS receptor binding research and melanocortin pathway studies in preclinical animal models.
Mitochondrial-derived peptide encoded within the mitochondrial genome. Emerging research target for metabolic pathway investigations, particularly AMPK-related signaling studies.
Synthetic tetrapeptide analogue of the naturally occurring pineal peptide epithalamin. Used as a research tool in studies examining telomerase expression and cellular lifespan in vitro.
Naturally occurring copper-binding tripeptide found in human plasma. Studied for its role in wound healing models, metalloproteinase modulation, and antioxidant activity in cell culture assays.
Every compound produced under the RIAN Peptides catalog undergoes a multi-stage quality verification protocol before release. Research integrity starts with compound integrity.
All peptides are produced via established Fmoc-SPPS methodology using pharmaceutical-grade protected amino acid building blocks. Coupling efficiency is monitored at each residue cycle.
Crude peptide material is subjected to preparative reverse-phase HPLC purification to achieve and verify target purity thresholds of 98% or greater prior to lyophilization.
Each batch undergoes ESI-MS or MALDI-TOF mass spectrometry confirmation to verify molecular weight and confirm correct amino acid sequence and structure.
Every compound ships with a batch-specific Certificate of Analysis documenting purity percentage, molecular weight confirmation, and storage recommendations for research use.
Lyophilized peptides are stored at controlled temperature conditions and shipped with appropriate cold-chain packaging to preserve compound stability during transit.
RIAN Peptides compounds conform to consistent quality specifications across the catalog. Custom synthesis and non-catalog compound requests are available to qualified research institutions.
| Parameter | Standard Specification |
|---|---|
| Purity Minimum | 98%+ HPLC |
| Synthesis Method | Fmoc Solid-Phase Peptide Synthesis (SPPS) |
| Verification | ESI-MS or MALDI-TOF mass spectrometry |
| Physical Form | Lyophilized powder unless otherwise specified |
| Counter Ion | Trifluoroacetate (TFA) or Acetate as noted |
| Storage Condition | -20°C, desiccated, protected from light |
| Reconstitution | Bacteriostatic water or sterile PBS per compound |
| Documentation | Batch-specific Certificate of Analysis included |
| Quantities Available | 1mg, 5mg, 10mg, 50mg, 100mg — bulk by request |
| Shipping | Cold-chain packaging, domestic and international |
| Intended Use | In vitro research and laboratory use only |
Submit a catalog inquiry, request a custom synthesis quotation, or contact our team to discuss compound availability and institutional research partnerships.