TB-500 is a synthetic peptide analog of Thymosin Beta-4, a naturally occurring intracellular protein encoded by the TMSB4X gene. Endogenous Thymosin Beta-4 is widely distributed in mammalian tissues and has been studied in laboratory research for its involvement in cell migration, cytoskeletal organization, and tissue related signaling pathways. TB-500 is engineered to support experimental investigation of similar biological mechanisms in controlled research environments.
Structurally, TB-500 is a 43-amino-acid peptide characterized by high water solubility and low molecular weight. In experimental models, Thymosin Beta-4 derived peptides have been examined for their interaction with actin dynamics, angiogenic signaling pathways, and cellular repair mechanisms. Research literature also explores their role in inflammatory signaling modulation and extracellular matrix interactions.
TB-500 has been detected in elevated concentrations within wound associated biological fluids, including platelet rich environments, leading researchers to investigate its relevance to tissue repair models. Additional laboratory studies have examined its association with neurological signaling, as well as cellular responses in experimental models involving cardiac, epidermal, and spinal tissue systems.
TB-500 is supplied strictly for laboratory and in vitro research use only. This compound is not intended for human or animal consumption, clinical use, diagnostic application, or therapeutic purposes.
Overview
TB-500, also referred to in research literature as a synthetic analog of thymosin, contains a functionally relevant peptide region spanning amino acids 17–23. This sequence has been examined in laboratory studies for its association with actin binding, cytoskeletal regulation, and cellular migration related signaling pathways.
The amino acid sequence of TB-500 is:
Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH
Actin proteins are fundamental components of the cellular cytoskeleton, playing critical roles in maintaining cell structure, intracellular transport, and motility. In experimental models, thymosin derived peptides have been studied for their interaction with globular actin (G-actin). This interaction has been examined for its potential to limit the polymerization of G-actin into filamentous actin (F-actin), a process often described as actin sequestration.
By influencing the balance between G-actin and F-actin, researchers investigate whether thymosin related peptides may alter cytoskeletal dynamics, cellular morphology, and movement under controlled laboratory conditions. These mechanisms are of interest in research areas where cell motility and structural remodeling are relevant experimental variables.
Thymosin has also been detected in extracellular environments, including plasma and wound associated fluids, prompting additional investigation into its role beyond intracellular activity. Experimental studies involving vascular and connective tissue cell models have examined whether extracellular thymosin may influence cell migration and angiogenic signaling pathways. Some research explores potential interactions with cell surface ATP synthase related systems, which are involved in cellular energy regulation.
Collectively, these findings support ongoing laboratory research into the intra and extracellular signaling roles of thymosin derived peptides and their influence on cytoskeletal organization and cellular communication.
TB500 is supplied strictly for research use only and is not intended for human or animal consumption, clinical application, diagnostic use, or therapeutic purposes.
