The short answer
TB-500 is a seven-residue acetylated peptide at 889.0 Da. Thymosin beta-4 is the 43-residue parent protein at 4,963 Da. They share the LKKTETQ motif, but much of the frequently cited wound-repair and cardiac literature used the full protein rather than the fragment.
Key facts
- TB-500
- 7 residues, 889.0 Da
- Thymosin beta-4
- 43 residues, 4,963 Da
- Shared
- The LKKTETQ actin-binding motif
- Motif position
- Residues 17–23 of Tβ4
- Actin work
- Applies to the motif
- Repair and cardiac work
- Largely used the full protein
The structural relationship
Thymosin beta-4's actin-binding activity concentrates in a short internal sequence, LKKTETQ, occupying residues 17 to 23. TB-500 is that sequence synthesised alone with an acetylated N-terminus. It is a fragment in the literal sense (a piece of the parent), and it retains the motif most directly associated with actin binding.
Why a fragment is not a small version of the protein
The other 36 residues are not padding. Thymosin beta-4 has reported activities beyond actin sequestration, and a protein's behaviour depends on its whole structure: how it folds, what surfaces it presents, what else it can contact. Isolating one functional motif keeps the activity attributable to that motif and discards everything attributable to the rest. Assuming the fragment reproduces the protein is an assumption, not a deduction.
Research material referenced
TB-500 5mg, third-party HPLC tested
Which literature applies to which
This is the practically important part. Actin-sequestration work is about the motif and transfers reasonably. The corneal wound-healing work reported by Sosne and colleagues, and the cardiac repair literature, largely used full-length thymosin beta-4. Citing that work as evidence about TB-500 the heptapeptide extends it beyond the molecule it was generated with.
Why the fragment is what is usually sold
Cost and difficulty. Seven residues is a routine solid-phase synthesis; 43 residues is a substantially harder one with more opportunity for deletion sequences and a higher price. The market settled on the fragment for practical reasons, and the name TB-500 followed it, while the literature people cite largely did not.
How to keep them straight
Ask what a study administered, not what the compound is called. Papers state the molecule they used. Where a paper used full-length thymosin beta-4 and a claim is being made about TB-500, the gap between them is a real one and worth noticing.
Quick reference
| TB-500 | Thymosin beta-4 | |
|---|---|---|
| Residues | 7 | 43 |
| Molecular weight | 889.0 Da | 4,963 Da |
| PubChem CID | 62707662 | 16132341 |
| CAS | – | 77591-33-4 |
| Contains LKKTETQ | Yes, it is the whole molecule | Yes (residues 17–23) |
| Synthesis | Routine | Substantially harder |
Frequently asked questions
- Does TB-500 do everything thymosin beta-4 does?
- Not established. It retains the actin-binding motif; the parent has reported activities beyond that, and the other 36 residues are not inert filler.
- Which was used in the wound-healing studies?
- Largely full-length thymosin beta-4, including the corneal work. That is a meaningful distinction when the findings are cited for the fragment.
- Why is the fragment sold instead of the protein?
- Seven residues is a routine synthesis; 43 is much harder and more expensive, with more scope for deletion sequences.
Extended research context
The TB-500 (Thymosin β4 fragment) deep dive
Deep dive: TB-500 vs full-length Thymosin Beta-4
'TB-500' is a synthetic peptide corresponding to the active 17-amino-acid actin-binding region of the endogenous 43-residue Thymosin Beta-4 protein. The two are not identical. TB-500 lacks the flanking sequence that gives full-length TB-4 additional binding partners. In the research literature, papers use 'Thymosin β4' when they mean the full protein and 'TB-500' or 'AcSDKP fragment' when they mean the shorter synthetic peptide. Reading a CoA carefully to see which molecule is in the vial matters. Mass spec is the definitive check.
Actin-binding as the core mechanism
The N-terminal region of TB-4 (and TB-500 by inheritance) contains the canonical actin-binding motif. This motif sequesters G-actin monomers, modulating the G:F actin equilibrium in cell cultures. That mechanism is why almost every mechanistic paper on TB-500 traces back to cytoskeletal reorganisation, cell migration, and models of tissue repair.
Handling considerations unique to TB-500
TB-500 is a 17-residue peptide with modest amphipathicity; it reconstitutes cleanly in bacteriostatic water but is sensitive to repeated freeze/thaw. Aliquoting into single-use volumes on first reconstitution preserves potency across a batch. HPLC on the batch CoA should show a single dominant peak; a doublet suggests deamidation.
Research applications
- ▸In vitro actin-polymerisation assays (G:F actin ratio measurement)
- ▸Cell-migration and wound-scratch assays in fibroblast lines
- ▸Angiogenesis models: tube-formation and endothelial migration assays
- ▸Analytical method development for short peptides on RP-HPLC
- ▸Reference-material comparisons against endogenous Thymosin β4
Handling checklist
- ✓Store lyophilised vials at −20 °C long-term
- ✓Reconstitute with bacteriostatic water (0.9% benzyl alcohol)
- ✓Aliquot immediately to avoid freeze/thaw cycles
- ✓Refrigerate reconstituted aliquots at 2–8 °C; use within 28 days
- ✓Confirm mass (~4,963 Da for TB-500) via CoA before study use
Common research-handling mistakes
Learnt from thousands of researcher orders across our UK labs.
✗ Assuming TB-500 = full Thymosin β4
Fix: TB-500 is the 17-residue actin-binding fragment; check the CoA sequence.
✗ Repeated freeze/thaw
Fix: Aliquot at first reconstitution; each cycle degrades yield.
✗ Using tap water
Fix: Use bacteriostatic or sterile water only.
Continue researching
Peer-reviewed guides, comparators and matched reference materials.
Related questions researchers ask
Primary sources & clinical trials
Peer-reviewed research and registered trials from PubMed, ClinicalTrials.gov, PubChem, FDA and NIH. All links open in a new tab and point to the primary source, so every claim can be verified at origin.
- PubMedLow TL et al., Complete amino acid sequence of bovine thymosin beta 4. PNAS 1981 (PMID 6940133)pubmed.ncbi.nlm.nih.gov
- PubMedSosne G et al., Thymosin beta 4 promotes corneal wound healing. Exp Eye Res 2002 (PMID 11950239)pubmed.ncbi.nlm.nih.gov
- PubMedHannappel E, beta-Thymosins: Ann N Y Acad Sci 2007 (PMID 17468232)pubmed.ncbi.nlm.nih.gov
- PubMedGoldstein AL et al., Thymosin β4: a multi-functional regenerative peptide. Expert Opin Biol Ther 2012 (PMID 22074294)pubmed.ncbi.nlm.nih.gov
- PubMedShrivastava S et al., Thymosin beta4 and cardiac repair. Ann N Y Acad Sci 2010 (PMID 20536454)pubmed.ncbi.nlm.nih.gov
- TrialClinicalTrials.gov · Thymosin β4 (RGN-259) dry eye Phase 3 (NCT03925727)clinicaltrials.gov
- PubChemPubChem · Thymosin β4 (CID 16132341)pubchem.ncbi.nlm.nih.gov
- PubMedNIH PubMed: Thymosin beta-4 tissue repairpubmed.ncbi.nlm.nih.gov
- GuidelineGoogle: Creating helpful, reliable, people-first contentdevelopers.google.com
Written and reviewed by
The UK Peptides Editorial Team · Research library, UK Peptides
The editorial team is responsible for supplier selection, batch release decisions and the content published in this research library. Every article here is sourced to primary literature and every product page to a signed third-party certificate. Corrections are made in place and the review date updated.
More TB-500 (Thymosin β4 fragment) articles
- Fragment or Full Protein: Which the Research UsesThe heptapeptide isolates the actin-binding motif; the full protein carries everything else. Which to use depends entirely on the question being asked.
- LKKTETQ: The Actin-Binding MotifLKKTETQ occupies residues 17–23 of thymosin beta-4 and carries its actin-binding activity. What the sequence does and why it was isolated.
- How Actin Sequestration WorksThymosin beta-4 binds monomeric G-actin and holds it out of filaments. Why maintaining a monomer pool matters for how quickly a cell can rebuild its skeleton.
- How Thymosin Beta-4 Was DiscoveredLow and colleagues published the complete sequence of bovine thymosin beta-4 in PNAS in February 1981, describing it as a thymic hormone. That framing changed.
- TB-500: Structure and Where It Comes FromSeven residues taken from the middle of a 43-residue protein, with an acetylated N-terminus. What that construction implies about its properties.
Popular across the research hub
One flagship guide from every other research category.
- Retatrutide ResearchRetatrutide Structure and Sequence
- GHK-Cu (Copper Peptide)The Molecular Structure of GHK and Its Copper Complex
- BPC-157 (Pentadecapeptide)BPC-157 Storage, Stability and Reconstitution
- CJC-1295 & IpamorelinStorage and Reconstitution for Both Compounds
- Peptide ReferencePeptide Terminology: The Words That Recur
- Bacteriostatic WaterThe Reason Preservative-Free Water Is a Separate Product
- Research & Regulatory News7,101 Participants, and No Answer Until 2027
- GLP-1 & Incretin ScienceWhen the Reason for Treatment Causes the Outcome
- MOTS-c (Mitochondrial Peptide)MOTS-c CAS Number and Chemical Identity
- Semax (ACTH Fragment Peptide)Semax Regulatory Status: Registered Where, and Why It Matters
- Selank (Tuftsin Analogue)Selank CAS Number and Chemical Identity
- DSIP (Delta Sleep-Inducing Peptide)The Missing Biology: No Gene, No Precursor, No Receptor
- KLOW (Blend)What You Can and Cannot Ask a Four-Component Blend
- GLOW (Blend)GLOW Regulatory Status
- MT-2 (Melanotan II)Two Compounds, One Parent, Opposite Intentions
- IGF-1 LR3Recombinant Versus Synthetic: Two Different Quality Problems
- GlutathioneGSH and GSSG: What the Ratio Measures
- NAD+The Membrane Problem: Why NAD+ Doesn't Get In
- KPVKPV Structure and Physical Properties