regenerative
TB-500
A synthetic peptide corresponding to the active domain of Thymosin Beta-4, investigated for its fundamental role in actin dynamics, cellular migration, and systemic tissue repair across cardiovascular and musculoskeletal research models.
For research and laboratory use only. Not for human consumption.
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Certificate of Analysis
Certificate of Analysis
COA documentation is being prepared for this product.
Contact research@roehnrx.com for batch-specific testing data.
Research Overview
About TB-500
TB-500 is a synthetic fragment encompassing the biologically active region of Thymosin Beta-4 (Tb4), a 43-amino-acid protein expressed in virtually every nucleated mammalian cell. The fragment retains the actin-binding domain responsible for the protein's influence on cytoskeletal organization — a process central to cell motility, wound closure, and tissue regeneration.
Research has established TB-500's capacity to sequester monomeric actin (G-actin), thereby regulating the polymerization dynamics that drive cell migration toward injury sites. This mechanism has been studied in the context of cardiac tissue recovery following ischemic events, skeletal muscle fiber regeneration, tendon remodeling, and endothelial cell proliferation during angiogenesis.
ROEHN's TB-500 is manufactured to 99% HPLC-verified purity and supplied as a lyophilized powder for maximum shelf stability. Its distinct mechanism of action — operating through cytoskeletal pathways rather than growth factor signaling — makes it a frequent companion to BPC-157 in combined-treatment research designs targeting connective tissue and soft tissue repair.
