Thymosin Beta-4 Fragment (TB4-Frag 17-23)
Also known as: TB4 fragment 17-23, TB-500 active peptide, LKKTETQ, thymosin beta-4 fragment, Ac-LKKTETQ
TB4-Frag is a research compound. Not approved for human use.
Overview
The heptapeptide fragment (amino acids 17–23) of full thymosin beta-4, sequence Ac-LKKTETQ. This sequence is the active actin-binding domain responsible for TB-500's tissue repair properties. Shorter molecular weight than TB-500 enables more targeted delivery while retaining identical mechanism of action on G-actin regulation and tissue repair signaling.
Research Summary
The LKKTETQ sequence was identified in 1994 as the minimum active fragment of thymosin beta-4 responsible for its actin-sequestering and tissue repair activity. This heptapeptide competes with actin monomer binding proteins, promoting cell migration, angiogenesis, and wound healing. Studies confirm it recapitulates the key bioactivity of full TB4 in cell migration and collagen deposition assays.
Dosing Range
low
250mcg
moderate
500mcg
high
1mg
Units: mcg–mg · Frequency: 2–3x weekly
Dosing ranges are aggregated from preclinical research and community protocols. Not medical dosing guidance.
Administration Routes
Reconstitution Notes
Reconstitute with bacteriostatic water. Target concentration: 500mcg/mL. Stable 28 days refrigerated. Smaller molecular weight than TB-500 — may be more easily dosed in smaller volumes.Step-by-step reconstitution guide →
Supplies you'll need
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Reported Side Effects
- Injection site irritation
- Mild fatigue (transient)
- Potential headache
- Generally well-tolerated in research applications
Research Papers
2 peer-reviewed sourcesCommunity Experiences
Aggregated from public forums. Anecdotal — not clinical evidence.
Community discussion comparing TB4-Frag 17-23 to full TB-500 in injury recovery protocols.
View original threadResearch and anecdotal reports on the minimum active fragment of TB4 for tissue repair.
View original threadOverview
TB4-Frag (fragment 17–23) is the scientifically identified minimum active fragment of thymosin beta-4 (TB4) — the parent molecule behind the popular research peptide TB-500. The full TB4 protein is 43 amino acids; researchers in the 1990s systematically mapped which portion of the molecule was responsible for its signature activity: binding G-actin (monomeric actin) and modulating the actin cytoskeleton.
The answer was the heptapeptide LKKTETQ (Leu-Lys-Lys-Thr-Glu-Thr-Gln), spanning positions 17–23. The N-acetylated form (Ac-LKKTETQ) is the research standard. This sequence contains the critical WH2 domain motif (GxxxQ) essential for G-actin binding across the actin-binding protein superfamily.
Mechanism
Actin-Dependent Healing
The fundamental mechanism of TB4 and its fragment is G-actin sequestration:
- G-actin binding: The LKKTET motif binds monomeric actin (G-actin) with high affinity, competing with profilin for actin monomers
- Cell migration promotion: By modulating the G-actin:F-actin ratio, the fragment promotes lamellipodia formation and directed cell migration — critical for wound healing
- Angiogenesis: Promotes endothelial cell migration and tubulogenesis, stimulating new blood vessel formation to healing tissue
- Anti-inflammatory signaling: Downregulates NFκB-mediated inflammatory cytokines (IL-1β, TNF-α) in injured tissue
- Fibroblast activation: Promotes fibroblast migration to injury site and collagen deposition
TB4-Frag vs. Full TB-500
| Parameter | TB4-Frag (17-23) | TB-500 | |-----------|-----------------|--------| | Amino acids | 7 | 43 (commercial: ~17-43) | | Molecular weight | ~800 Da | ~4,900 Da | | G-actin binding | Yes (direct) | Yes (via same domain) | | Non-actin domains | Absent | Present | | Bioavailability | Potentially higher | Standard | | Half-life | Shorter | Longer |
Research Context
The TB4-frag approach is based on the principle that the minimum effective sequence is sufficient — avoiding any activities residing in other TB4 domains. However, some researchers argue the full TB4 (or the commercial TB-500 fragment 17–43) may have additive effects from non-actin binding domains involved in immunomodulation. Both approaches have legitimate research rationales.
Combination Protocols
TB4-Frag is commonly studied in the "Wolverine Stack" alongside BPC-157:
- BPC-157: Drives angiogenesis and upregulates growth factor receptors (VEGFR, FGFR)
- TB4-Frag / TB-500: Regulates actin dynamics for cell migration into the injury site
These mechanisms are non-overlapping and complementary, making the combination a logical research pairing for comprehensive tissue repair investigation.
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