
Thymosin Beta-4 Fragment (17–23)
A synthetic fragment of Thymosin Beta-4 researched for tissue repair, cell migration, and anti-inflammatory activity — most evidence is from animal models, with human trials limited to topical ophthalmic use of the full protein.
A synthetic fragment of Thymosin Beta-4, a protein found in nearly every cell in the body and released in high concentrations at wound sites. Studied for tissue repair, reducing inflammation, and promoting new blood vessel growth into injured areas. The rodent evidence for healing is solid. Human trials exist for the full protein administered as eye drops — not for the injectable fragment used by researchers. Often paired with BPC-157 because they act through different but complementary pathways. The same VEGF/cancer concern that applies to BPC-157 applies here.
Half-Life
Not established for injectable fragment in humans. One Phase I study of full injectable Tβ4 showed dose-proportional PK with no accumulation at repeated dosing (PMID: 34346165).
Molecular Weight
895 Da (fragment) / 4963 Da (full Tβ4)
TB-500 is a synthetic peptide corresponding to the actin-binding fragment of Thymosin Beta-4 (Tβ4), a naturally occurring 43-amino-acid protein found in high concentrations in platelets and wound fluid. The fragment retains the actin-sequestration domain of full Tβ4 and is researched for tissue repair, cell migration, and anti-inflammatory activity — primarily in rodent models. Human clinical trials exist for full Tβ4 administered topically for corneal conditions; no published human trials exist for injectable TB-500 fragment for musculoskeletal or systemic use. The two are not interchangeable: TB-500 is a fragment (~895 Da), Tβ4 is the full protein (~4963 Da). Many vendors sell either interchangeably under the "TB-500" label — the COA molecular weight distinguishes them.
Also Known As
Amino Acid Sequence
Ac-Lys-Pro-Asp-Met-Ala-Glu-Ile (Fragment 17–23 core; full Tβ4: 43 aa)
Reconstitution
Reconstitute with bacteriostatic water. Typical concentration: 1 mg/mL.
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