All products are for laboratory research use only. Not for human consumption.
Tissue Repair · Tissue Recovery
The Healing Catalyst
RM 250
Unlock your body’s natural fluidity. TB-500 10mg activates cellular migration, encouraging deep tissue renewal and ageless vitality.
For research use only. Not for human or veterinary consumption. This product is not a medicine and is not intended to diagnose, treat, cure or prevent any disease.
Overview
Thymosin Beta-4 (TB-4) is the naturally occurring full-length 43-amino-acid endogenous peptide produced in virtually all nucleated cells. Unlike the TB-500 fragment, TB-4 contains the complete sequence including the N-terminal domain (direct immunomodulation), the C-terminal domain (additional actin regulation), and the ILK-binding domain validated in Phase 2 cardiac trials. Per molecule, it is significantly more potent than the TB-500 fragment.
Mechanism of action
Complete actin-binding regulation across all relevant domains
Direct T-cell and macrophage modulation — not present in TB-500
Integrin-linked kinase activation for cardiac repair — human trial data
Key finding TB-4 full-length activates integrin-linked kinase (ILK), which drives cardiac cell migration and survival after injury. This mechanism was published in Nature (2004) and validated in Phase 2 clinical trials — representing the strongest cardiac repair evidence of any tissue repair peptide.
Key research findings
TB-4 directly binds and activates integrin-linked kinase (ILK) — driving cardiac cell migration and survival
Bock-Marquette I et al. Nature, 2004TB-4 completed Phase 2 cardiac trial demonstrating cardiomyocyte migration and cardiac repair enhancement
Cardiac Phase 2 dataFull-length TB-4 directly modulates T-cell and macrophage activity — activity absent from TB-500 fragment
Goldstein AL et al. Expert Opin Biol Ther, 2012Full-length TB-4 promotes oligodendrocyte differentiation and myelin formation — not replicated by fragment
Hannappel E. Ann N Y Acad Sci, 2007Research areas
The strongest cardiac repair peptide data available — Phase 2 clinical data validating the ILK/Akt mechanism published in Nature.
Direct immunomodulatory activity unique to full-length TB-4 — not available with TB-500 fragment.
Full-length TB-4 promotes oligodendrocyte differentiation and myelination — neural repair activity beyond TB-500.
Complete actin regulatory sequence with broader tissue coverage than the TB-500 fragment.
Safety profile
TB-4 full-length has the same general safety profile as TB-500, with additional immunomodulatory activity to consider. Phase 2 cardiac trial safety data available.
VEGFR2 and angiogenic activity — note in oncology research contexts
Direct immune cell modulation — additional to TB-500 activity
ILK pathway activation — account for cardiac signaling in research designs
Prohibited by WADA — S0 category applies to TB-4 and all fragments
Molecular profile
Frequently asked questions
Integrin-linked kinase (ILK) is a serine-threonine kinase that acts downstream of integrins at cell adhesion sites. TB-4 directly binds and activates ILK, which then phosphorylates Akt (a master cell survival kinase). In cardiac tissue, ILK/Akt activation drives cardiomyocyte survival after ischemia and promotes cell migration for cardiac repair. This mechanism was published in Nature in 2004 by Bock-Marquette et al.
TB-4 directly modulates T-cell differentiation and activation, macrophage polarization between M1 (inflammatory) and M2 (repair) phenotypes, and NK cell activity. These effects are mediated by the N-terminal and C-terminal domains of TB-4 that are not present in the LKKTET actin-binding fragment (TB-500). The thymus is the primary natural source of TB-4 — consistent with immunomodulatory function.
TB-4 completed a Phase 2 clinical trial for cardiac repair in patients who had experienced myocardial infarction. The trial evaluated TB-4’s ability to promote cardiac repair via the ILK/Akt pathway. Safety and efficacy data from this trial are available. Multiple earlier human studies focused on wound healing applications.
References
