TB-500
Stylized molecular signature · scaled by MW
Full-length Tβ4 ~2.5 h plasma t½ in rodents; product literature commonly sells full-length Tβ4 (4963 Da) under the 'TB-500' label, though the true active fragment (LKKTETQ, ~889 Da) has a t½ <30 min. MW reflects full-length Tβ4 as marketed.
Profiled for reference only.
TB-500 is indexed here for literature reference. Peptide Plus does not list this compound at the time of this page generation. Peptide Plus remains the seller of record for any compound listed on alphapeptide.store — we do not ship, store, or handle product.
How it’s studied.
Thymosin Beta-4 is a 43-residue G-actin-sequestering peptide that maintains the monomeric actin pool in eukaryotic cells. The central LKKTETQ heptapeptide motif (residues 17-23) mediates actin binding and is sufficient for most extracellular regenerative activity — including upregulation of laminin-5 in keratinocytes, induction of endothelial cell migration via Ac-SDKP cleavage products, and modulation of the PI3K/Akt and ILK signaling axes. Studied for angiogenesis, cardiomyocyte survival post-MI, corneal repair, and dermal wound healing.
TB-500 is the commercial designation for Thymosin Beta-4, a 43-amino-acid actin-binding peptide ubiquitous in mammalian cells. Originally isolated from calf thymus, it has emerged as a leading regenerative research tool, with the heptapeptide LKKTETQ identified as the minimal active fragment driving wound-healing, angiogenic, and anti-inflammatory effects.
- 01
Myocardial infarction and cardiomyocyte survival models
- 02
Corneal and dermal wound-healing studies
- 03
Skeletal muscle and tendon repair research
- 04
Hair follicle stem-cell migration assays
Reported in literature: 2–10 mg/kg IV or SC in rodent cardiac studies; veterinary protocols 2–2.5 mg/week (clinical research, not for human use)
Verify each value in primary literature.
Pre-filled defaults for TB-500.
- Concentration
- 2.50mg/mL
- Draw on U-100
- 400units
- Volume / dose
- 4.000mL
- Doses / vial
- 0
Assumes 27-gauge insulin syringe, U-100 markings. Verify before use.
Open in calculatorCo-factors and supporting compounds.
Moderate evidenceCompounds identified in published research as sharing pathways with TB-500, or studied alongside it in trials. Reference material only — not a recommendation, not medical advice. Citations link to PubMed.
Zinc
ZincZinc-dependent MMP catalysis required for TB-4 matrix remodelling
Thymosin beta-4 has been reported to upregulate matrix metalloproteinases MMP-1, MMP-2, and MMP-9 in keratinocytes, endothelial cells, fibroblasts, and activated monocytes during wound repair, with the activity localized to the LKKTET central actin-binding domain. MMPs are a family of zinc-dependent endopeptidases — the catalytic site requires a zinc ion — so the matrix-remodelling arm of TB-4 biology is intrinsically gated by zinc availability. Systemic zinc adequacy is therefore a documented permissive cofactor for the proteolytic component of TB-4-driven tissue repair, even though TB-4 itself does not bind zinc. Animal and cell-culture evidence.
Vascular endothelial growth factor (VEGF) and the angiogenic axis
VEGF (endogenous effector, not a supplement)VEGF/Akt-driven angiogenesis and endothelial progenitor survival
Thymosin beta-4 has been reported to upregulate VEGF expression and to drive endothelial-cell migration, tubular formation, and survival via PI3K/Akt and Notch signalling. In a rat MI model, TB-4 pretreatment of endothelial progenitor cells before transplantation improved ejection fraction, reduced scar, and raised microvessel density, with phospho-Akt elevated. This is a mechanistic-cofactor entry rather than a supplement-stacking one: VEGF is the downstream effector that mediates much of TB-4's regenerative output, which is why TB-4 research is often paired with angiogenesis read-outs and progenitor-cell protocols. Animal-model evidence.
Vitamin C (L-ascorbic acid)
AscorbateCollagen hydroxylation required for granulation tissue maturation in TB-4 wound models
Ascorbate is the obligate cofactor for prolyl and lysyl hydroxylases that hydroxylate collagen precursors so the triple helix can fold and be cross-linked. Thymosin beta-4 has been studied across dermal, corneal, and burn wound-healing models in which collagen deposition and granulation tissue maturation are primary endpoints — the same biosynthetic chain that requires ascorbate. Vitamin C is therefore a permissive cofactor for the collagen-deposition arm of TB-4 driven repair, even though the two have not been formally co-administered in published TB-4 protocols. Co-administration is a plausible research stacking choice in dermal-repair contexts.
TB-4 literature is large (~800 PubMed entries) but cofactor co-administration studies are sparse. Zinc is a permissive cofactor because MMPs are zinc-dependent enzymes; VEGF is a mechanistic effector rather than a supplement. Vitamin D was searched and not found in any TB-4 co-administration context, so it was excluded to avoid fabrication.