If you have been reading about actin-binding motif 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.
Last reviewed on 2026-05-02. Where a claim depends on a specific study, the study is described rather than over-claimed.
Lyophilised material is stable for extended periods when kept dry and cold, and suppliers typically recommend storage well below freezing. Once dissolved, the peptide is handled at refrigeration temperatures and used within a short period, because peptide bonds and the acetylated terminus can be affected by repeated freeze-thaw cycles, proteases, or extreme pH. Bacteriostatic water and saline are both described as solvents, although preservatives can interfere with some analytical workflows. Reconstituted solutions are inspected for particulates before use.
Sports authorities classify the peptide as a prohibited substance, and it appears on the World Anti-Doping Agency list under peptide hormones, growth factors, and related substances. Racing jurisdictions for horses and dogs have issued separate restrictions, and several national bodies treat it as a controlled or prescription-only item. As a research chemical it is sold without a therapeutic indication, and labels usually state that the product is not for human or veterinary use. Regulatory treatment therefore varies by country.
Detection in biological matrices generally relies on liquid chromatography coupled with tandem mass spectrometry, because the peptide lacks a convenient ultraviolet chromophore beyond the amide backbone. Immunoassays have been described, but antibodies raised against the fragment can cross-react with the full-length protein or with unrelated peptides, so findings usually require confirmation by a second technique. Sample preparation typically involves protein precipitation followed by solid-phase extraction. Reported detection windows depend on dose, route, matrix, and instrument sensitivity.
TB-500 is a synthetic seven-amino-acid peptide with the sequence LKKTETQ, corresponding to residues 17 through 23 of the protein thymosin beta-4. The N-terminus is typically acetylated in the described form, giving a monoisotopic mass near 888.5 Da and an average mass of about 889 Da. The designation TB-500 is a catalogue label rather than a formal chemical name, and the same sequence appears in the literature under several alternative abbreviations. It is handled as a research reagent rather than a pharmaceutical product.
Thymosin beta-4 is a 43-residue actin-binding protein found in most mammalian cell types, where it participates in cytoskeletal regulation and cell migration. TB-500 represents only a short fragment of that protein and does not include the remaining residues. Whether the isolated fragment reproduces the full range of activities reported for the intact protein remains an open question. Researchers commonly treat the two as related but distinct entities when comparing results.
Published work involving this sequence spans actin-binding assays, cell-migration studies, wound-healing models, and cardiovascular or musculoskeletal experiments. Much of the biological rationale derives from in vitro systems and animal models, and the number of controlled human studies is small. Reported outcomes vary across preparations, doses, and routes, which complicates comparison between studies. Reviews generally describe the evidence base as preliminary rather than settled. Mechanistic explanations are often proposed by analogy to the parent protein rather than demonstrated directly.
| Property | Value | Notes |
|---|---|---|
| Analytical method | LC-MS/MS | Preferred confirmatory technique |
| Appearance | White to off-white powder | Lyophilised form |
| Solubility | Freely soluble in water | Also described in saline |
| Storage temperature | Below -20 °C for powder | Short-term refrigeration for solutions |
| Regulatory status | Prohibited in sport | Listed under peptide hormones |
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.
Peptide bonds are susceptible to hydrolysis under extreme pH and to enzymatic cleavage if proteases are present. Heat, oxidising agents, and prolonged exposure to light also contribute to loss of material. Aggregation can occur at high concentrations or in certain buffer systems, and it may not be visible to the eye. Storage at -20 C or below is typical for both powder and aliquoted solutions, and desiccation of the powder is preferred.
Identity and purity are usually assessed by reversed-phase high-performance liquid chromatography together with mass spectrometry. The chromatogram provides a purity estimate as a percentage of total peak area, while the mass spectrum confirms that the observed mass matches the expected value. Amino acid analysis or tandem mass spectrometry sequencing can provide additional confirmation. Reported purity figures depend on the column, gradient, and detection wavelength, so values from different laboratories are not directly comparable without method details.
Identity and purity are checked with reversed-phase high-performance liquid chromatography, which separates the target sequence from truncated or deletion analogues, and with mass spectrometry, which confirms the expected molecular mass. Amino acid analysis and peptide mapping give orthogonal confirmation but are used less often outside specialist laboratories. Counter-ion content varies: material purified on trifluoroacetic acid gradients retains trifluoroacetate, and ion exchange can convert the salt form. Residual water and solvent are measured by Karl Fischer titration or thermogravimetric analysis, and any purity figure should be read together with the method used to obtain it.
Lyophilised peptide powders are hygroscopic, and the fragment absorbs atmospheric moisture when a vial is opened at room temperature. Weighing and aliquoting are normally done quickly in a dry environment, and stock solutions are divided into single-use portions before freezing. Repeated freeze-thaw cycles are avoided because they promote aggregation and can shift the measured content of a vial. These practices are general to synthetic peptides rather than unique to this sequence, but they matter more for short chains kept for long periods.
The seven-residue chain carries several polar and charged side chains, so it dissolves readily in water and in aqueous buffers near neutral pH. No cysteine is present, so disulphide formation is not a concern and reducing agents are unnecessary. Dilute ammonium hydroxide or acetonitrile-water mixtures are sometimes used for stock solutions when initial dissolution is slow. Strongly alkaline conditions and prolonged contact with oxidising agents are avoided because they can modify lysine-containing stretches, and haze in solution usually signals incomplete dissolution or aggregated material.
Uranium–lead radiometric dating involves using uranium-235 or uranium-238 to date a substance's absolute age. This scheme has been refined to the point that the error margin in dates of rocks can be as low as less than two million years in two-and-a-half billion years. An error margin of 2–5% has been achieved on younger Mesozoic rocks. Uranium–lead dating is often performed on the mineral zircon (ZrSiO4), though it can be used on other materials, such as baddeleyite and monazite (see: monazite geochronology). Zircon and baddeleyite incorporate uranium atoms into their crystalline structure as substitutes for zirconium, but strongly reject lead. Zircon has a very high closure temperature, is resistant to mechanical weathering and is very chemically inert. Zircon also forms multiple crystal layers during metamorphic events, which each may record an isotopic age of the event. In situ micro-beam analysis can be achieved via laser ICP-MS or SIMS techniques. One of its great advantages is that any sample provides two clocks, one based on uranium-235's decay to lead-207 with a half-life of about 700 million years, and one based on uranium-238's decay to lead-206 with a half-life of about 4.5 billion years, providing a built-in crosscheck that allows accurate determination of the age of the sample even if some of the lead has been lost. This can be seen in the concordia diagram, where the samples plot along an errorchron (straight line) which intersects the concordia curve at the age of the sample.
Granulocyte colony-stimulating factor (G-CSF or GCSF), also known as colony-stimulating factor 3 (CSF 3), is a glycoprotein that stimulates the bone marrow to produce granulocytes and stem cells and release them into the bloodstream. Functionally, it is a cytokine and hormone, a type of colony-stimulating factor, and is produced by a number of different tissues. The pharmaceutical analogs of naturally occurring G-CSF are called filgrastim and lenograstim. G-CSF also stimulates the survival, proliferation, differentiation, and function of neutrophil precursors and mature neutrophils.
In the example of lysosomal lipase, the enzyme is confined within an organelle called the lysosome. Other lipase enzymes, such as pancreatic lipases, are secreted into extracellular spaces where they serve to process dietary lipids into more simple forms that can be more easily absorbed and transported throughout the body. Fungi and bacteria may secrete lipases to facilitate nutrient absorption from the external medium (or in examples of pathogenic microbes, to promote invasion of a new host). Certain wasp and bee venoms contain phospholipases that enhance the effects of injury and inflammation delivered by a sting. As biological membranes are integral to living cells and are largely composed of phospholipids, lipases play important roles in cell biology. Malassezia globosa, a fungus thought to be the cause of human dandruff, uses lipase to break down sebum into oleic acid and increase skin cell production, causing dandruff. Genes encoding lipases are even present in certain viruses. Some lipases are expressed and secreted by pathogenic organisms during an infection. In particular, Candida albicans has many lipases, possibly reflecting broad-lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue.
Sources: en.wikipedia.org
Camurus is a company focused on the development of lipid lyotropic liquid crystal structures for pharmaceutical drug delivery applications. These structures are well-defined three-dimensional formations consisting of lipophilic and hydrophilic domains that can be either interconnected or isolated depending on the environmentally induced phase conditions. The unique crystalline structures offer a unique way of encapsulating and transporting Active pharmaceutical ingredients, such as small molecules, peptides and proteins through the body. The structures also allow for the use of controlled release and prevention of degradation of fragile short half live molecules, a serious issue for amino-acid based drugs.
Naturally occurring rhenium (75Re) is 37.4% 185Re, which is stable (although it is predicted to decay), and 62.6% 187Re, which is unstable but has a very long half-life (4.16×1010 years). Among elements with a known stable isotope, only indium and tellurium similarly occur with a stable isotope in lower abundance than the long-lived radioactive isotope. There are 36 other unstable isotopes recognized, the longest-lived of which are 183Re with a half-life of 70 days, 184Re with a half-life of 35.4 days, 186Re with a half-life of 3.7185 days, 182Re with a half-life of 64.2 hours, and 189Re with a half-life of 24.3 hours. There are also numerous isomers, the longest-lived of which are 186mRe with a half-life of 200,000 years and 184mRe with a half-life of 177.25 days. All others have half-lives less than a day.
The cell's energy is equal to the voltage times the charge. Each gram of lithium represents Faraday's constant / 6.941(atomic mass), or 13,901 coulombs. At 3 V, this gives 41.7 kJ per gram of lithium, or 11.6 kWh per kilogram of lithium. This is slightly more than the heat of combustion of gasoline; however, lithium-ion batteries as a whole are still significantly heavier per unit of energy due to the additional materials used in production. Note that the cell voltages involved in these reactions are larger than the potential at which an aqueous solutions would electrolyze.
Sources: en.wikipedia.org
The most common approach is liquid chromatography with tandem mass spectrometry after extraction from blood or urine. Immunoassays exist but are generally treated as screening tools because of cross-reactivity.
Dry lyophilised powder is normally kept frozen and protected from moisture and light. Dissolved material is handled cold and used promptly to limit degradation.
It is not licensed as a medicine in major markets and is distributed as a research chemical. Sports organisations prohibit its use, and some countries restrict import and supply.
No. TB-500 is a short synthetic peptide matching residues 17 to 23 of thymosin beta-4, while the parent protein contains 43 residues. The fragment lacks the rest of the protein sequence, so the two are related but not identical.