TB-500 (Thymosin β4 fragment)

TB-500 vs Thymosin Beta-4

UKPWritten & reviewed by The UK Peptides Editorial Team · Research library, UK Peptides2 min readLast reviewed 2026-08-233 cited sources

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

Buy TB-500 · £23.99

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-500Thymosin beta-4
Residues743
Molecular weight889.0 Da4,963 Da
PubChem CID6270766216132341
CAS–77591-33-4
Contains LKKTETQYes, it is the whole moleculeYes (residues 17–23)
SynthesisRoutineSubstantially 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.

UKP

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.

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