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TB-500 (Thymosin Beta-4)
TB-500, derived from the naturally occurring protein Thymosin Beta-4, is a synthetic peptide that binds to a protein called actin, which is involved in the formation of new blood vessels and the repair of damaged tissues.
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Laborergebnisse ansehen →TB-500, derived from the naturally occurring protein Thymosin Beta-4, is a synthetic peptide that binds to a protein called actin, which is involved in the formation of new blood vessels and the repair of damaged tissues. By binding to actin, TB-500 helps stimulate the growth of new blood vessels and promotes the formation of new tissue functions.
The ability of TB-500 to reduce inflammation and promote cell migration, proliferation, and differentiation, which can help to facilitate tissue repair and regeneration has been demonstrated in various research. It is currently studied for its potential to enhance athletic performance and improve recovery from injury.
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3D Molecular Structure
Drag to rotate · scroll to zoomTb-500-thymosin-beta-42mg 1 vial | 2mg 10 vials | 5mg 1 vial | 5mg 10 vials | 10mg 1 vial | 10mg 10 vials
| Chemical Formula | C212H350N56O78S |
|---|---|
| Synonyms | Thymosin Beta-4, Tβ4 |
| Molar Mass | 4693 g/mol |
| CAS Number | 77591-33-4 |
| PubChem CID | 16132341 |
| Total Compound Content | 10 mg per vial |
| Shelf Life | 36 months |
TB-500 is a 43-amino-acid synthetic analogue of Thymosin Beta-4 (Tβ4) that has been extensively investigated for its interactions with actin-regulatory systems. Its primary characterized mechanism involves G-actin monomer sequestration through the conserved LKKTET motif (residues 17–23), influencing actin polymerization dynamics, actin filament assembly, and cytoskeletal organization. Experimental investigations have examined the relationship between TB-500 and actin-associated protein interactions, cytoskeletal signaling networks, and molecular processes governing structural protein organization.
Additional research has explored the influence of TB-500 on signaling pathways associated with actin regulation, protein interaction networks, intracellular structural dynamics, and pathway-specific regulatory mechanisms. These investigations have contributed to the characterization of TB-500 as a useful tool for studying actin-binding activity, cytoskeletal architecture, structure-function relationships, and peptide-mediated regulation of actin-associated signaling systems.
Results refer to the tested sample. Check the batch and date in the report.
TB-500 (Thymosin Beta-4) 5mg (GC-MS/LC-MS Contamination Screening)
June 18, 2026
What is the primary mechanism by which TB-500 influences actin-regulatory systems?
TB-500 interacts with G-actin monomers through the conserved LKKTET motif (residues 17–23), influencing actin sequestration, actin filament assembly, and polymerization dynamics. This mechanism has made TB-500 a valuable research tool for investigating actin-associated protein interactions, cytoskeletal organization, and the molecular processes governing structural protein regulation.
What signaling pathways have been associated with TB-500 in experimental investigations?
Research involving TB-500 has examined its relationship with actin-associated signaling networks, protein interaction pathways, and regulatory mechanisms involved in cytoskeletal organization. These investigations have contributed to the characterization of TB-500 as a useful tool for studying actin-dependent signaling, intracellular structural dynamics, and pathway-specific regulatory processes.
Why is TB-500 frequently used in cytoskeletal research?
TB-500 possesses a well-characterized actin-binding mechanism and a defined interaction with actin-regulatory systems. Its ability to influence actin polymerization dynamics, cytoskeletal architecture, and protein interaction networks has established it as a widely utilized reference compound in studies examining structural protein organization, actin-associated signaling pathways, and peptide structure-function relationships.
Customer Reviews (10)
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Quick and easy shopping experience. The product arrived on time and as described.
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