TB-500 Research Guide
5mg · Research compound — not for human consumption
Research Overview
TB-500 is a synthetic peptide fragment modeled on Thymosin Beta-4 (Tbeta4), a naturally occurring 43-amino-acid actin-binding protein. It has been studied in preclinical and in vitro settings for its role in actin regulation and cell-migration models. TB-500 is not FDA-approved and is presented here solely as a research compound not intended for human consumption.
Structural & Class Overview
Synthetic peptide fragment derived from the Thymosin Beta-4 sequence; the parent Tbeta4 is a G-actin-sequestering peptide (parent PubChem CID 45382195). Mechanistically classed among actin-modulating/cytoskeletal-remodeling peptides that interact with globular (G) actin and influence the G-actin/F-actin equilibrium.
General Research Interest
Research interest includes G-actin sequestration and cytoskeletal-remodeling dynamics; endothelial cell organization and migration in wound-model assays; angiogenesis-related actin-binding protein expression; and tissue-repair signaling explored across preclinical injury models. These represent laboratory study areas, not established human benefits.
Storage Considerations
General research-handling notes for a lyophilized peptide: keep the sealed lyophilized material cold, dry, and protected from light per supplier documentation; after reconstitution for laboratory use, refrigerate and limit freeze-thaw cycles. For laboratory settings only. Not intended for human consumption.
Testing & Quality Considerations
Quality considerations include HPLC purity analysis, mass-spectrometry confirmation of identity and molecular mass, and review of a batch-specific Certificate of Analysis (COA) prior to research use.
References
- Thymosin Beta 4 — PubChem CID 45382195
- Nuclear localisation of the G-actin sequestering peptide thymosin beta4 (PubMed)
- Thymosin beta 4 and Fx, an actin-sequestering peptide (PubMed)
References are provided for scientific context. Linked sources are independent and not affiliated with iNGEN MD.
