TB-500 Australia

TB-500 Australia. TB-500 is the cell movement and wound repair peptide. Because its mechanism underlies movement generally, the reported outcomes spread wide: faster wound closure, less fibrosis and better remodelling of scar tissue, new blood vessel growth, and recovery of heart and corneal tissue in injury models. The soft tissue work reports faster tendon, ligament and muscle repair and better flexibility, and a separate strand covers hair follicles.

How it does it. TB-500 is the research market name for thymosin β-4, a peptide occurring naturally in almost every cell in the body. Its job is managing actin, the protein filaments forming a cell's internal scaffolding. It binds loose actin building blocks and holds them in reserve, which is what lets a cell take its own skeleton apart and rebuild it somewhere else. That is how cells crawl toward damaged tissue.

The vial. Independently HPLC-tested by Janoshik, with the certificate of analysis published on this page and in the lab-reports library, carrying the measured number and a verifiable Janoshik key. Supplied in 5 mg and 10 mg freeze-dried vials, dispatched from Australia, AUD pricing. Supplied strictly for in-vitro and laboratory research use only. Not for human or animal consumption, not a therapeutic good, not TGA-approved.

Also written tb500 and thymosin beta-4. TB500 without the hyphen, tb500 australia and thymosin beta 4 all name the same 43 residue actin-binding peptide as the vials above. They are supplied at 5 mg and 10 mg, each with its own Janoshik certificate.

TB-500 (CAS 77591-33-4; molecular formula C212H350N56O78S, average molecular weight ≈ 4963 g/mol) is thymosin β-4 — a 43-residue, N-terminally acetylated peptide that binds and sequesters monomeric G-actin, making it a central regulator of actin dynamics in research models. Although the name “TB-500” historically referred to a short active fragment of the molecule, in the research-peptide market it is used for the full-length thymosin β-4 peptide — the form referenced here and reflected in the certificate of analysis.

The molecular identity of thymosin β-4 as the actin-sequestering peptide was established by Safer and colleagues (Journal of Biological Chemistry, 1991), who showed Tβ4 and the actin-sequestering peptide “Fx” are indistinguishable; Sanders and colleagues (Proceedings of the National Academy of Sciences, 1992) then demonstrated that it regulates actin-polymerisation dynamics inside living cells.

The broader actin-binding biochemistry and its downstream tissue-repair, cell-migration and angiogenesis research are surveyed in the review by Goldstein and colleagues (Expert Opinion on Biological Therapy, 2012). TB-500 is studied across actin-dynamics, cell-migration, tissue-repair, angiogenesis and inflammation-modulation research literature.

TB-500 is most frequently referenced alongside BPC-157 in the canonical "soft-tissue" research stack — the two compounds act on distinct pathways (actin dynamics versus growth-factor / nitric-oxide signalling) that converge on the tissue-repair research model. See the BPC-157 + TB-500 research blend product page for the co-lyophilised research-stack variant.

The information provided here is a research-reference summary only. Elite AU Peptides makes no medical, therapeutic, performance, or human-use claim about this product. TB-500 is not TGA-approved, is not a therapeutic good, and is supplied strictly for in-vitro and laboratory research use only. Researchers should consult the primary peer-reviewed literature for actin-binding data and protocol-specific reference values.

Reconstitute the lyophilised TB-500 vial with bacteriostatic water for laboratory handling. Add the diluent slowly down the vial wall and swirl gently rather than shaking. The required volume depends on the protocol’s downstream assay requirements — a 5 mg vial reconstituted in 2 mL of bacteriostatic water yields a 2.5 mg/mL working stock; a 10 mg vial reconstituted in 5 mL yields a 2 mg/mL working stock. Adjust per protocol.

Store the lyophilised powder at −20°C, desiccated and protected from light; once reconstituted, store refrigerated at 2–8°C and use within the documented research window, or aliquot and freeze to avoid repeated freeze-thaw cycles. Tamper-evident packaging; the batch label is the canonical reference for the certificate of analysis published in the lab-reports library.

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30-day returns on unused product in original packaging, with prior approval.