Selank is a synthetic linear heptapeptide originally developed by researchers from the Institute of Molecular Genetics of the Russian Academy of Sciences. It is a stabilized structural analog of tuftsin, a natural tetrapeptide derived from the Fc fragment of immunoglobulin G with innate immunomodulatory activity. The native tuftsin molecule is rapidly degraded by proteases in biological environments; by adding a C-terminal Pro-Gly-Pro tripeptide sequence, Selank gains greatly improved enzymatic resistance and extended stability for preclinical experimental applications.

Selank is widely used in neuroimmunology, neuropharmacology and cognitive function laboratory research. In preclinical models, Selank exerts multimodal regulatory effects on central nervous system signaling pathways. It modulates GABAergic neurotransmission and the expression of GABA-A receptor related genes, demonstrating anxiolytic effects in animal anxiety assays without inducing sedation, physical dependence or withdrawal symptoms commonly seen with benzodiazepine compounds. It also inhibits enkephalin-degrading peptidases to preserve endogenous enkephalin levels, and regulates monoamine neurotransmitters including serotonin, dopamine and norepinephrine. Multiple research papers have documented its capacity to upregulate BDNF (brain-derived neurotrophic factor) expression within the hippocampus and prefrontal cortex, making it a valuable reagent for investigating neuroplasticity, memory consolidation and stress response mechanisms.

Beyond central neuroregulatory research, Selank retains the immunomodulatory characteristics inherited from tuftsin. It participates in the regulation of cytokine release such as IL-6, modulates the activity of macrophages and other immune effector cells, and supports research on neuroimmune crosstalk, inflammatory balance and stress-induced immune dysfunction.

Our Selank peptide is manufactured using solid-phase peptide synthesis (SPPS). After peptide chain assembly and deprotection steps, crude material undergoes preparative high-performance liquid chromatography purification to remove truncated fragments, residual protecting groups and related impurities. Each production batch is verified by mass spectrometry (MS) to confirm molecular identity, and HPLC analysis is performed to validate purity. Additional quality control tests include moisture content, residual solvent, heavy metal screening and microbial limit inspection. Batch-specific COA documents containing HPLC chromatogram and MS spectrum can be supplied upon request. The lyophilized powder formulation protects peptide integrity during transit and long-term cold storage. Once reconstituted, the peptide solution should be aliquoted immediately. Short-term storage can be maintained at 2–8°C, while long-term preservation requires -20°C storage. Repeated freeze-thaw cycles must be avoided to prevent peptide breakdown and loss of biological activity.