If you have been reading about Thymosin beta-4 and want a single page that covers the useful parts, this is it: definitions, context, how it is studied, and the questions that come up repeatedly.
Updated 2026-02-05. Numbers and descriptions here follow the published literature rather than marketing material.
Proposed activity centers on actin sequestration and on the movement of cells during repair processes. In cell culture and animal models, the fragment has been associated with migration, tube formation, and tissue remodeling. These observations are frequently described as preliminary, because most published work uses rodent or in vitro systems rather than controlled human trials. Whether the short fragment reproduces the effects of the full protein remains an open question, and the relationship between dose, route, and measured outcome is not well characterized.
The compound circulates in the literature as a research reagent rather than an approved therapeutic. Regulatory agencies in several countries have not authorized it for medical use, and sporting bodies list related thymosin beta-4 peptides among prohibited substances. Suppliers typically market it with a purity figure and a certificate of analysis, while peer-reviewed clinical reports remain sparse. Discussions therefore often separate laboratory findings from anecdotal reports, and reviewers tend to note the small size and methodological limits of the available studies.
The compound is most often distributed as a lyophilized powder, appearing white to off-white and forming a loose cake or fluffy solid. It is hygroscopic to some degree, so brief exposure to humid air can add water weight and complicate weighing. The peptide dissolves readily in water and in neutral aqueous buffers, and aqueous solubility is generally described as high, well above the concentrations used in typical assays. Some polar organic solvents are also usable, which matters when a concentrated stock is prepared before dilution into buffer.
Storage recommendations center on keeping the dry powder cold, dry, and dark. A freezer at -20 degrees Celsius or below is conventional, and desiccant is often included to limit moisture uptake. Once dissolved, the peptide is less stable, and solutions are typically kept frozen and thawed only once. Repeated freeze-thaw cycles are a common source of losses because they promote aggregation and adsorption to container surfaces. Working aliquots are therefore prepared in advance, and glass or low-binding plastic is usually preferred over ordinary laboratory plastic.
Identity and purity are assessed with a small set of standard techniques. Reverse-phase high-performance liquid chromatography gives a purity estimate from peak area, usually recorded at 214 or 220 nanometers, where the peptide bond absorbs. Mass spectrometry confirms the expected molecular mass and can reveal truncated or oxidized species. Amino acid analysis or tandem mass spectrometry sequencing can verify the sequence itself. Additional quality attributes include water content, residual trifluoroacetic acid carried over from purification, and endotoxin where the material is intended for biological work.
| Property | Value | Notes |
|---|---|---|
| Appearance | White to off-white powder | Lyophilized solid as supplied |
| Water solubility | Soluble | Dissolves in aqueous media |
| Typical storage temperature | -20 °C | Dry powder, desiccated, protected from light |
| Typical analytical method | RP-HPLC with mass spectrometry | Purity from peak area; mass for identity |
| Common synonyms | Tβ4 fragment; thymosin beta-4 fragment | Naming varies by supplier and catalogue |
TB-500 is a research peptide whose sequence matches residues 17 to 23 of thymosin beta-4, a 43-residue protein present in most mammalian cells. The chain is seven amino acids long, written as LKKTETQ, and is normally supplied with an acetyl group on the N-terminus. Suppliers list it as a lyophilised powder under the code name TB-500, and the same sequence appears elsewhere in catalogues as the thymosin beta-4 actin-binding fragment. The label is commercial rather than systematic, so no single authority fixes exactly what TB-500 denotes.
Thymosin beta-4 was isolated from calf thymus in the early 1980s and later characterised as an abundant intracellular actin-sequestering protein. Interest in short synthetic fragments grew once the actin-binding motif had been mapped to the middle of the sequence. TB-500 came out of that line of work as a truncated analogue rather than a natural isolate, and it is now sold mainly to laboratories. Published studies on the fragment have been largely in vitro or in animal models, and controlled human trials remain sparse, so claims about effects in people rest on extrapolation.
Literature and online discussion often conflate TB-500 with full-length thymosin beta-4, even though the two differ in size and are not interchangeable in analytical terms. The fragment is produced by solid-phase peptide synthesis, and the product is a defined seven-residue chain rather than a biological extract. Because the term is a trade-style label, two vendors may supply materials of the same nominal sequence but different counter-ion content, purity, or water content. Comparisons across studies are therefore difficult unless the exact sequence and purity are reported.
The most frequently cited identity is a seven-residue fragment with the sequence LKKTETQ, taken from the actin-binding domain of the parent protein. A separate molecule, N-acetyl-seryl-aspartyl-lysyl-proline, often shortened to Ac-SDKP, derives from the same protein's N-terminal region and appears in overlapping literature. Reported molecular masses therefore differ between sources, and a mass value on its own does not establish which fragment is present. Confirmation requires a defined sequence rather than a single number.
Research interest in thymosin beta-4 fragments centres on actin sequestration, cell migration and tissue repair models. Most published work uses cultured cells or animal wound and cardiac preparations, and findings are generally described as preliminary. No fragment of this protein has been approved as a therapeutic product by major regulators. Reviews of the field note inconsistent dosing, delivery routes and outcome measures across studies, which complicates direct comparison. The material is best understood as a laboratory reagent with an active but unresolved research literature.
where Ni is the number of molecules of molecular mass Mi. The mass average molecular mass can be determined by static light scattering, small angle neutron scattering, X-ray scattering, and sedimentation velocity. The ratio of the mass average to the number average is called the dispersity or the polydispersity index. The mass-average molecular mass, Mw, is also related to the fractional monomer conversion, p, in step-growth polymerization (for the simplest case of linear polymers formed from two monomers in equimolar quantities) as per Carothers' equation:
=== Origins === LLNL was established in 1952, as the University of California Radiation Laboratory, Livermore Branch, an offshoot of the existing University of California Radiation Laboratory at Berkeley. The lab at Livermore was intended to spur innovation and provide competition to the nuclear weapon design laboratory at Los Alamos in New Mexico, home of the Manhattan Project that developed the first atomic weapons. The Livermore facility was co-founded by Edward Teller and Ernest Lawrence, director of the Radiation Laboratory at Berkeley. The new laboratory was sited at a former naval air station from World War II. It was already home to several University of California Radiation Laboratory projects that were too large for its location in the Berkeley Hills above the UC campus, including one of the first experiments in the magnetic approach to confined thermonuclear reactions (i.e. fusion). About half an hour southeast of Berkeley, the Livermore site provided much greater security for classified projects than an urban university campus. Lawrence tapped his former graduate student Herbert York, age 32, to run Livermore. Under York, the Lab had four main programs: Project Sherwood (the magnetic-fusion program), Project Whitney (the weapons-design program), diagnostic weapon experiments (both for the Los Alamos and Livermore laboratories), and a basic physics program. York and the new lab embraced the Lawrence "big science" approach, tackling challenging projects with physicists, chemists, engineers, and computational scientists working together in multidisciplinary teams.
== Activity == Given its half-life, the radioactive activity of a gram of 60Co is close to 42 TBq (1,100 Ci). The absorbed dose constant, used in calculations of gamma-ray exposure, is related to the decay energy and time. For 60Co it is equal to 0.35 mSv/(GBq h) at one meter from the source. This allows calculation of the equivalent dose, which depends on distance and activity - for example, 2.8 GBq or 60 μg of 60Co, generates a dose of 1 mSv at 1 meter away, within an hour. Test sources, such as those used for school experiments, have an activity of <100 kBq. Devices for nondestructive material testing use sources with activities of 1 TBq and more. The decay energy of cobalt-60 amounts to about 26 watts per gram, about 40 times larger (by mass) than that of e.g. 238Pu but still not very significant for practical sources.
Sources: en.wikipedia.org
== Prognosis == The life expectancy of patients with homocystinuria is reduced only if untreated. It is known that before the age of 30, almost one quarter of patients die as a result of thrombotic complications (e.g., heart attack).
=== Casein allergy === A small fraction of the population is allergic to casein. Casein intolerance, also known as "milk protein intolerance", is experienced when the body cannot break down the proteins of casein. The prevalence of casein allergy or intolerance ranges from 0.25% to 4.9% of young children. Numbers for older children and adults are not known. Casein that is heat-treated has been shown to be more allergenic and harder to digest when fed to infants. Breast milk has not been shown to cause an allergic reaction typically, but should be administered to an infant with caution each time in case of adverse reaction from something the breastfeeding parent consumed that contained casein. Following a casein-free diet has been shown to improve outcomes of infants who are breastfed while allergic or intolerant to dairy protein. Supplementation of protease enzyme has been shown to help casein intolerant individuals digest the protein with minimal adverse reaction.
On December 15, 2020, the acquisition was completed, and Dunkin' Brands ceased to exist as a separate company, with Dunkin', Baskin-Robbins, and the trademark management of Mister Donut, becoming part of Inspire Brands. In May 2026, Dunkin' current parent company Inspire Brands signed a franchise agreement with Montreal-based holding company Foodtastic to bring the restaurant chain back to Canada eight years after the company ceased its operations in the North. Peter Mammas, the president and CEO of restaurant holding company Foodtastic said its return this time will be different, and that this time the chain’s focus will be on Canadian ownership. Mammas expects the first Dunkin’ cafes to open in Canada later this year. A year from now, he says the company will likely be able to open a cafe a week, and about 50 cafes a year. “We have boots on the ground, so we’re going to have local support to support the franchises,” he said. He also said the company will concentrate on opening stores in Quebec and Ontario for the first two years before opening cafes in the Maritimes and the West Coast.
Sources: en.wikipedia.org
TB-500 is a name used for a short synthetic peptide fragment taken from the actin-binding region of thymosin beta-4. Material sold under this label is usually a lyophilized powder supplied for laboratory research rather than a licensed medicine. The commonly cited sequence is LKKTETQ.
The parent protein contains forty-three amino acids, while the fragment carries only a short motif from one region. The fragment can interact with actin in vitro, but it does not include the rest of the protein structure. Whether the shorter molecule behaves the same way in living systems is not settled.
Published controlled human studies are scarce, and most activity reports come from cell culture or animal models. Reviews often describe the evidence base as limited and methodologically uneven. Open questions include the relationship between route, dose, and measured outcomes.
Short transit at ambient temperature is generally tolerated, but long-term storage at room temperature is not recommended. Heat, moisture, and light all accelerate degradation. Cold, dry, dark storage is the conventional choice.