Thymalin

Thymalin is a synthetic polypeptide bioregulator derived from the thymus gland, developed by Vladimir Khavinson's group at the Saint Petersburg Institute of Bioregulation and Gerontology as the minimal active sequence from thymus extracts (Thymalinum). As one of the peptide bioregulators in Khavinson's research programme, Thymalin represents the thymic peptide analogue alongside pineal (Epithalon), cortical (Cortagen), and cardiovascular (Cardiogen) bioregulators.

The thymus gland is the primary organ of T lymphocyte maturation. Thymic peptides — including Thymosin Alpha-1, Thymalin, and related compounds — have been studied as immunomodulatory agents that restore age-related thymic involution-associated immune deficits. The thymus undergoes progressive involution from puberty onwards, substantially reducing naive T cell output by middle age and contributing to immunosenescence.

Thymalin's immunological research profile includes effects on T lymphocyte maturation and differentiation markers, NK cell activity, interferon production, and interleukin signalling in immune cell culture models. Published research from Khavinson's institute has examined Thymalin in aged rodent models examining immune function restoration and lifespan effects.

The mechanistic basis proposed for Thymalin's activity follows the Khavinson bioregulator hypothesis: short tissue-derived peptides act as epigenetic regulators, restoring gene expression patterns in target tissues that decline with age. For Thymalin, the target tissue is thymic epithelial cells, with proposed restoration of thymosin and thymulin production that drives T cell maturation.

Research applications include T cell proliferation and differentiation assays (CD4/CD8 ratio, naive vs memory T cell markers), NK cell cytotoxicity assays, cytokine production measurement (IL-2, IL-6, interferon-gamma by ELISA), thymic epithelial cell culture models, and comparison with Thymosin Alpha-1 (the clinically used thymic peptide) in parallel immunological research paradigms.

MW: approximately 1400-1500 Da (polypeptide mixture). Reconstitute in bacteriostatic water at 1mg/mL. Store lyophilised at -20°C. For laboratory and analytical research purposes only.

Hexarelin cardiac biology research: the cardiac binding site for Hexarelin — distinct from GHS-R1a — has been studied using CD36 (fatty acid translocase/thrombospondin receptor) as the proposed cardiac hexarelin receptor. Research examining this mechanism uses: CD36-expressing versus CD36-deficient cardiomyocytes (or CD36 siRNA knockdown) to assess whether cardiac hexarelin effects are CD36-dependent; 125I-hexarelin radioligand binding assays on cardiac membrane preparations before and after anti-CD36 antibody pre-incubation; and pharmacological controls using a GHS-R1a antagonist (to block pituitary GHS-R1a) while preserving cardiac CD36 binding.

For GH axis comparative research: primary rat anterior pituitary cells prepared by enzymatic digestion and density gradient separation. Seed at 100,000 cells/well in 24-well plates. After 48-hour recovery, treat with Hexarelin, GHRP-2, GHRP-6, and Ipamorelin at matched molar concentrations (correct for MW differences: Hexarelin 887.05, GHRP-2 817.94, GHRP-6 873.03, Ipamorelin 711.85 g/mol). Collect medium at 15, 30, 60, and 120 minutes. Measure GH (rat GH ELISA), ACTH (rat ACTH ELISA), and prolactin (rat prolactin ELISA) in parallel from the same time-point samples. Calculate GH:ACTH and GH:prolactin selectivity ratios for each compound. Hexarelin should show the highest absolute GH release and lowest selectivity ratios; Ipamorelin should show similar or lower GH release but highest selectivity ratios. MW: 887.05 g/mol. CAS: 140703-51-1. Contains tryptophan — store at -20°C, amber container. For laboratory and analytical research purposes only.