Peptide Insider Research Desk · Published 2026-09-22 · Compound review; companion to the TB-500 / thymosin β4 research review and the BPC-157 / TB-500 blend review
Few nomenclature questions recur in research-peptide catalogues as often as the identity question behind tb500 vs tb4, tb-500 thymosin beta-4 and is tb4 the same as tb500. The short answer from the primary literature is that they are related but not identical: thymosin β4 (Tβ4, gene TMSB4X, UniProt P62328) is a 43-residue, N-terminally acetylated, highly acidic actin-sequestering protein [1, 2], whereas the label TB-500 is applied in analytical and catalogue literature to a synthetic peptide reproducing the seven-residue actin-binding motif LKKTETQ at residues 17–23 of Tβ4, usually with N-terminal acetylation [6, 15]. Every compound named is strictly for research reference; not for human or veterinary use.
Definition. Thymosin β4 is the most abundant member of the β-thymosin family of small acidic G-actin-sequestering peptides; the human protein is 43 amino acids (Ac-SDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES), ~4.9 kDa, encoded by TMSB4X (UniProt P62328) [2, 4, 5]. "TB-500" is a catalogue and analytical-chemistry label for a synthetic fragment corresponding to the Tβ4 actin-binding domain, residues 17–23 (LKKTETQ), characterised in doping-control mass spectrometry as "a synthetic version of an active region of thymosin β4" [15]. Ac-SDKP is the N-terminal tetrapeptide released from Tβ4 by prolyl oligopeptidase [12]. All three are strictly for research reference; not for human or veterinary use.
Why the TB-500 / Thymosin β4 Identity Question Matters
In brief: Thymosin β4 and TB-500 differ by 36 residues and roughly 4 kDa. The full protein sequesters G-actin through a central LKKTETQ motif [3, 6]; TB-500 is that motif synthesised alone [15]. Conflating the two mis-assigns forty years of Tβ4 literature to a seven-residue fragment that has its own, much thinner, evidence base.
The distinction is not pedantic. Almost every mechanistic paper cited for "TB-500" in secondary sources studied the intact 43-residue protein: wound-closure models used recombinant or synthetic full-length Tβ4 [8], the cardiac migration and survival experiments used full-length Tβ4 [9, 10], and the corneal epithelial studies likewise used the whole protein [11]. Only a small subset of experiments tested the 17–23 fragment directly, and those are the papers that speak to TB-500 as a compound in its own right [6, 7]. A researcher who searches tb4 vs tb500 peptide is therefore asking a literature-mapping question: which findings transfer from the parent protein to the fragment, and which do not.
Catalogue orthography compounds the problem. "TB4", "Tβ4", "TB-4" and "thymosin beta 4" denote the protein; "TB-500", "TB500" and "tb 500" denote the fragment product; and mixed strings such as tb-500 thymosin beta-4 or thymosin beta 4 tb 500 are written by users who assume synonymy.
Thymosin β4: The 43-Residue Actin-Sequestering Protein (TMSB4X, UniProt P62328)
In brief: Thymosin β4 is a 43-amino-acid, N-acetylated, intrinsically disordered peptide (~4.9 kDa) that binds monomeric G-actin 1:1 and is present at up to 0.5 mM in many mammalian cells; it was sequenced in 1981 and identified as the actin-sequestering factor Fx in 1991 [2, 3, 4].
Low, Hu and Goldstein reported the complete 43-residue sequence of bovine thymosin β4 in 1981 [2]. Huff and colleagues' review documents the family's defining properties: small (40–44 residues), acidic (pI ~5), N-terminally acetylated, lacking stable secondary structure in aqueous solution, and binding ATP-G-actin with micromolar affinity to buffer the cytosolic monomer pool [4].
Goldstein, Hannappel and Kleinman's 2005 review coined the "moonlighting" framing: an intracellular actin-sequestering protein that, when released or applied extracellularly, participates in cell migration, angiogenesis and tissue repair in experimental models [1]. Crockford et al. summarise the structure–function map: an N-terminal region containing the Ac-SDKP sequence, a central actin-binding motif spanning residues 17–23, and a C-terminal region whose contribution to cell-binding was defined by peptide-mapping studies [13].
The LKKTETQ Actin-Binding Motif (Residues 17–23) and Its Synthetic Fragment
In brief: LKKTETQ is the seven-residue central motif of Tβ4 that contacts actin. Philp et al. showed in 2003 that the synthetic heptapeptide alone reproduces the parent protein's pro-angiogenic activity in endothelial migration and in vivo Matrigel models, whereas a scrambled sequence does not [6].
The critical experiment for the identity question is Philp, Huff, Gho, Hannappel and Kleinman (2003): synthetic peptides spanning the actin-binding site, including the seven-residue LKKTETQ, promoted human umbilical-vein endothelial cell migration and vessel formation in a Matrigel plug assay to a degree comparable with full-length Tβ4, while peptides from other regions and a scrambled control were inactive [6].
Sosne, Qiu, Goldstein and Wheater (2010) extended the peptide-mapping approach, testing a panel of short synthetic Tβ4 sequences across corneal epithelial migration, anti-inflammatory and cytoprotection read-outs. Their conclusion is central to any tb500 vs tb4 comparison: the biological activities of Tβ4 are partitioned among distinct short sequences. The actin-binding heptapeptide carried the migration activity, the N-terminal Ac-SDKP region carried other activities, and no single short fragment reproduced the whole activity profile of the intact protein [7].
TB-500 as a Catalogue Label: What the Analytical-Chemistry Literature Records
In brief: The most authoritative published description of TB-500 is from equine doping-control chemistry: Ho et al. (2012) characterise TB-500 as a synthetic version of an active region of thymosin β4 and describe its detection by LC-MS in equine urine and plasma [15]. TB-500 is not a pharmacopoeial name.
Unlike Tβ4, which has a gene symbol, a UniProt accession and four decades of biochemistry, "TB-500" has no entry in any nomenclature authority. The label appears in the peer-reviewed record almost exclusively through analytical chemistry. Ho and colleagues at the Hong Kong Jockey Club Racing Laboratory developed a liquid chromatography–mass spectrometry method for TB-500 in horse urine and plasma, defined its precursor and product ions, and studied its in-vitro and in-vivo metabolites, explicitly describing the analyte as a synthetic fragment corresponding to an active region of Tβ4 [15]; a later multi-analyte horse-plasma screen included it among seven bioactive peptides [16].
The practical consequence for a research catalogue is that the chemical identity of a vial labelled TB-500 is established by sequence and mass spectrometry, not by name. The expected identity is the N-acetylated heptapeptide Ac-Leu-Lys-Lys-Thr-Glu-Thr-Gln (Ac-LKKTETQ), with a monoisotopic mass of roughly 889 Da; a certificate of analysis that reports a 43-residue, ~4.9 kDa product is describing Tβ4, not TB-500. The identifier-first verification approach is developed in the vendor-independent quality-verification review and the supplier-evaluation guide; no vendor is assessed or endorsed here.
Ac-SDKP: The N-Terminal Tetrapeptide Metabolite
In brief: Ac-SDKP (N-acetyl-seryl-aspartyl-lysyl-proline) is residues 1–4 of Tβ4, released by prolyl oligopeptidase and degraded by angiotensin-converting enzyme; it is a third, distinct entity that catalogue searches for "TB4" sometimes conflate with both the protein and TB-500 [5, 12].
Cavasin's 2006 review sets out the relationship: Tβ4 is the sole known precursor of Ac-SDKP in mammalian tissue, the tetrapeptide is cleaved from the acetylated N-terminus by prolyl oligopeptidase, and it is hydrolysed by the N-domain of ACE, which is why ACE-inhibitor exposure raises circulating Ac-SDKP in experimental systems [12]. For nomenclature purposes: TB-500 (residues 17–23) and Ac-SDKP (residues 1–4) do not overlap in sequence, and neither is a synonym for the parent protein.
Side-by-Side: Thymosin β4 vs TB-500 vs Ac-SDKP
In brief: Three entities, one gene. The protein is 43 residues and actin-binding; TB-500 is the isolated 7-residue actin-binding motif; Ac-SDKP is the 4-residue N-terminus with no actin affinity. The table fixes each by sequence, mass and identifier so that the comparison can be checked against a certificate of analysis.
| Property | Thymosin β4 (Tβ4, "TB4") | TB-500 | Ac-SDKP |
|---|---|---|---|
| Residue span of Tβ4 | 1–43 (entire protein) | 17–23 | 1–4 |
| Sequence | Ac-SDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES | Ac-LKKTETQ (typically N-acetylated) | Ac-SDKP |
| Approximate mass | ~4.96 kDa [2, 4] | ~0.89 kDa (heptapeptide) | ~0.49 kDa |
| Persistent identifier | UniProt P62328; gene TMSB4X | None (analytical/catalogue label) [15] | None as entity; defined as Tβ4(1–4) [12] |
| Actin binding | Yes, 1:1 G-actin sequestration [3, 4] | Contains the actin-binding motif; reproduces migration/angiogenesis activity in vitro [6] | No [12] |
| Primary literature depth | Extensive (biochemistry, rodent, zebrafish, one Phase-1 safety study) [1, 9, 10, 14] | Peptide-mapping studies plus doping-control analytics [6, 7, 15, 16] | Cardiovascular and renal fibrosis models [12] |
| Correct catalogue label | Thymosin β4 / Tβ4 / TB4 | TB-500 (Tβ4 17–23 fragment) | Ac-SDKP |
Evidence by Entity: Research Model and Signal Vector
In brief: The evidence is asymmetric. Intact Tβ4 has been studied from actin biochemistry to a randomised Phase-1 safety study; the 17–23 fragment has direct evidence only in endothelial and epithelial in-vitro mapping and a Matrigel model; Ac-SDKP has its own cardiovascular literature.
| Entity · domain | Research model | Signal vector | Primary literature |
|---|---|---|---|
| Tβ4 · actin sequestration | Platelet extracts; purified actin | 1:1 G-actin binding; identity of Tβ4 with Fx | [3, 4] |
| Tβ4 · dermal wound closure | Rat full-thickness wounds; db/db mice | Accelerated re-epithelialisation, keratinocyte migration | [8] |
| Tβ4 · cardiac repair | Mouse coronary ligation; embryonic cardiac explants | ILK/Akt activation; cardiomyocyte survival; migration | [9] |
| Tβ4 · epicardial progenitors | Adult mouse heart explants | Epicardium-derived cell mobilisation; neovascularisation | [10] |
| Tβ4 · corneal epithelium | Human corneal epithelial cells | Internalisation-dependent anti-apoptotic effect | [11] |
| Tβ4 · human safety (Phase 1) | Randomised placebo-controlled volunteers | Tolerability and pharmacokinetics recorded; no efficacy claim | [14] |
| Tβ4(17–23) / TB-500 · angiogenesis | HUVEC migration; Matrigel plug | Heptapeptide reproduces parent migration/vessel-forming activity | [6] |
| Tβ4 fragments · activity partition | Corneal epithelial and inflammatory assays | Distinct short sequences carry distinct activities | [7] |
| TB-500 · analytical identity | Equine urine and plasma LC-MS | Precursor/product ions; metabolite profile | [15, 16] |
| Ac-SDKP · fibrosis | Rodent infarct and hypertension models | Anti-fibrotic; ACE-dependent clearance | [12] |
BPC-157 vs TB-500: Two Distinct Peptides Often Co-Listed
In brief: BPC-157 and TB-500 share nothing at the sequence level. BPC-157 is a 15-residue fragment (GEPPPGKPADDAGLV) of a gastric-juice protein studied mainly by the Zagreb group [17]; TB-500 is the 7-residue actin-binding motif of Tβ4 [6, 15]. Their frequent co-listing is a catalogue convention, not a mechanistic relationship.
The string bpc157 vs tb500 and the blend vocabulary around it (bpc 157 and tb500 blend, tb 500 bpc 157 blend, bpc tb 500 blend, tb500 bpc 157 blend) arise because catalogues co-formulate the two peptides in a single lyophilised vial. Sikiric et al. describe BPC-157 as a stable gastric pentadecapeptide with a wide preclinical literature in gastrointestinal, tendon and vascular models [17]; none of that literature involves Tβ4 or its fragments, and none of the Tβ4 literature involves BPC-157. Co-formulation chemistry, oral dosage-form terminology and the catalogue "blend" concept are treated in the BPC-157 / TB-500 blend review and the catalogue-formats review.
Catalogue-Vocabulary Crosswalk: Query String → Resolved Entity → Identifier → RUO Scope Status
In brief: Each recurring search string is recorded verbatim and resolved to the protein, the 17–23 fragment, the BPC-157 co-listing or a declined category. Strings that encode mixing, stacking or protocol intent are recorded as vocabulary and declined for content.
| Query string (verbatim) | Intent class | Resolved entity | RUO scope status |
|---|---|---|---|
| tb500 vs tb4 | Comparison question | Tβ4 (P62328) vs Tβ4(17–23) fragment | Recorded-as-nomenclature; answered above |
| tb4 vs tb 500 | Comparison; whitespace variant | Same as above | Recorded-as-orthographic-variant |
| tb4 vs tb500 peptide | Comparison; 'peptide' suffix | Same as above | Recorded-as-orthographic-variant |
| is tb4 the same as tb500 | Question form | No: 43-residue protein vs 7-residue fragment [6, 15] | Recorded-as-nomenclature; answered in FAQ |
| tb-500 thymosin beta-4 | Compound pairing | TB-500 = Tβ4(17–23); Tβ4 = P62328 | Recorded-as-nomenclature (assumed synonymy corrected) |
| thymosin beta 4 tb 500 | Compound pairing; unhyphenated | Same as above | Recorded-as-orthographic-variant |
| tb 500 thymosin | Truncated pairing | Same as above | Recorded-as-orthographic-variant |
| bpc157 vs tb500 | Comparison question | BPC-157 (pentadecapeptide) vs TB-500 | Recorded-as-nomenclature; answered above |
| bpc 157 and tb500 blend | Blend vocabulary | BPC-157 + TB-500 co-formulation | Recorded-as-catalogue-terminology |
| tb 500 bpc 157 blend | Blend vocabulary; order reversed | Same | Recorded-as-catalogue-terminology |
| bpc tb 500 blend | Blend vocabulary; truncated | Same | Recorded-as-catalogue-terminology |
| tb500 bpc 157 blend | Blend vocabulary | Same | Recorded-as-catalogue-terminology |
| bpc-157 & tb-500 blend | Blend vocabulary; ampersand | Same | Recorded-as-catalogue-terminology |
| peptides bpc 157 and tb500 | Family pairing | Same | Recorded-as-catalogue-terminology |
| bpc-157 and tb-500 peptides | Family pairing | Same | Recorded-as-catalogue-terminology |
| bpc 157 peptide and tb 500 | Family pairing | Same | Recorded-as-catalogue-terminology |
| bpc 157 and tb 500 peptides | Family pairing | Same | Recorded-as-catalogue-terminology |
| bpc 157 and tb500 peptides | Family pairing | Same | Recorded-as-catalogue-terminology |
| peptides tb500 bpc157 | Family pairing; order reversed | Same | Recorded-as-catalogue-terminology |
| tb500 and bpc-157 | Pairing | Same | Recorded-as-catalogue-terminology |
| tb500 and bpc157 | Pairing; unhyphenated | Same | Recorded-as-catalogue-terminology |
| bpc 157 plus tb 500 | Pairing; 'plus' | Same | Recorded-as-catalogue-terminology |
| bp 157 tb500 | Truncation error (bp for bpc) | BPC-157 + TB-500 | Recorded-as-orthographic-error |
| bp 157 tb 500 | Truncation error; spaced | Same | Recorded-as-orthographic-error |
| boc 157 tb 500 | Transposition error (boc for bpc) | Same | Recorded-as-orthographic-error |
| wolverine bpc-157 & tb-500 | Community nickname | BPC-157 + TB-500 | Recorded-as-community-vocabulary only |
| bpc 157 peptide/tb 500 wolverine stack | Nickname + 'stack' (protocol intent) | — | Declined-protocol; vocabulary recorded only |
| bpc-157 and tb-500 mixed together | Co-formulation / mixing intent | — | Declined-preparation-guidance; see blend review for chemistry vocabulary |
| how to mix bpc 157 and tb 500 | Preparation instruction | — | Declined-preparation-guidance |
| bpc 157 tb 500 oral | Dosage-form descriptor | Oral peptide dosage-form literature | Recorded-as-dosage-form-terminology; no use guidance |
Handling and Stability Notes
In brief: Tβ4 and TB-500 are both acidic-to-neutral, lyophilised peptides whose main degradation routes are deamidation (Gln, Asn), oxidation of the single Met6 in Tβ4, and adsorption; the heptapeptide lacks Met and is less prone to oxidation but carries a C-terminal Gln susceptible to deamidation [18].
Manning et al. catalogue the chemical and physical instabilities relevant to any peptide reagent: deamidation, oxidation, hydrolysis, aggregation and surface adsorption [18]. Reconstitution-media vocabulary is covered in the bacteriostatic-water review and container-adsorption issues in the syringes and needles consumables review. Nothing here is preparation or use guidance.
Limitations of the Underlying Literature
In brief: The identity of TB-500 with Tβ4(17–23) rests on analytical papers and vendor convention rather than on a nomenclature authority; the fragment's biological data are limited to in-vitro and Matrigel systems; and the parent protein's repair literature, while broad, is largely preclinical.
Two caveats bound the conclusions; the only human data cited is a Phase-1 tolerability study [14], and this article makes no efficacy claim and provides no dosing guidance. First, "TB-500" has no authoritative definition, so a given catalogue product could in principle deviate from Ac-LKKTETQ; the identity stated here is the one recorded in the doping-control literature [15, 16]. Second, the direct evidence for the heptapeptide comes from a small number of peptide-mapping studies [6, 7]; extrapolating the parent protein's cardiac, dermal and corneal findings [8–11] to the fragment is not supported by the primary record.
Related Peptide Insider Reviews
The Tβ4 family sits at the intersection of several clusters already reviewed on this site. Links are grouped by axis.
- Tβ4 family and blends: TB-500 / thymosin β4 research review · BPC-157 / TB-500 blend review · KLOW blend (GHK-Cu / BPC-157 / TB-500 / KPV) · KPV component nomenclature review
- BPC-157 cluster: BPC-157 tissue-repair review · BPC-157 stability and catalogue nomenclature
- Copper and repair peptides: GHK-Cu copper tripeptide review · Copper peptides family review · GHK-Cu topical formulation and GLOW blend
- Other precursor-derived fragments: LL-37, kisspeptin-10, ARA-290 and PEG-MGF · HGH fragment 176-191 and the somatotropic axis · Thymosin alpha 1 (a distinct thymosin)
- Nomenclature and orthography: Query-orthography crosswalk review · CJC-1295 with vs without DAC · MK-677 is not a peptide
- Sourcing, quality and handling: How to evaluate research peptide suppliers · Vendor-independent quality verification · Bacteriostatic water and reconstitution media · Buffered vs unbuffered NAD+ reconstitution chemistry
Where to Source for Research
Researchers comparing catalogue listings for thymosin β4, TB-500 or BPC-157 can review the research-reagent offerings and certificates of analysis from several suppliers: Short Chain Aminos, BioPep, Catalyst Research and Apex Research Services. Listings should be checked against the identifiers in this review, above all the residue count and mass on the certificate of analysis, which distinguish a 43-residue Tβ4 product from a 7-residue TB-500 fragment. This is a statement of research availability, not a recommendation; all materials are strictly for research reference; not for human or veterinary use.
Frequently Asked Questions
Is tb4 the same as tb500?
No. Thymosin β4 (Tβ4, TB4) is the 43-residue, ~4.9 kDa actin-sequestering protein encoded by TMSB4X (UniProt P62328) [2, 4]. TB-500 is a catalogue and analytical label for a synthetic 7-residue fragment, Ac-LKKTETQ, corresponding to residues 17–23 of Tβ4 [6, 15]. The fragment contains the actin-binding motif but is not the whole protein.
What does tb500 vs tb4 mean in the research literature?
The comparison contrasts the intact protein with its central actin-binding fragment. Philp et al. showed the heptapeptide reproduces Tβ4's endothelial migration and Matrigel angiogenesis activity [6], while Sosne et al. showed that other Tβ4 activities map to other short sequences [7], so the fragment captures part, not all, of the parent's profile.
What is tb-500 thymosin beta-4?
The string pairs two names that are often assumed to be synonyms. In the analytical literature TB-500 is described as 'a synthetic version of an active region of thymosin β4' [15]; thymosin β4 itself is the full-length protein first sequenced by Low, Hu and Goldstein in 1981 [2].
How does bpc157 vs tb500 differ?
BPC-157 is a 15-residue gastric pentadecapeptide (GEPPPGKPADDAGLV) with its own preclinical literature [17]; TB-500 is the Tβ4 17–23 fragment [6, 15]. They share no sequence and no documented mechanistic relationship; their pairing in catalogues (bpc 157 and tb500 blend, tb 500 bpc 157 blend) is a co-formulation convention.
What is Ac-SDKP and is it TB-500?
Ac-SDKP is the N-terminal tetrapeptide (residues 1–4) of Tβ4, released by prolyl oligopeptidase and cleared by ACE [5, 12]. It is not TB-500 (residues 17–23) and does not bind actin.
Does bpc 157 tb 500 oral describe a research dosage form?
It is a dosage-form descriptor used in catalogue listings. Oral dosage-form terminology is recorded in the catalogue-formats review; this article provides no use or dosing guidance and records the string as vocabulary only.
Are thymosin β4, TB-500 or BPC-157 approved for any use?
None of the three is referenced here for any use. The only human data cited is a Phase-1 tolerability study of intravenous Tβ4 [14], which makes no efficacy claim. All compounds are strictly for research reference; not for human or veterinary use.
Works Cited
- Goldstein AL, Hannappel E, Kleinman HK. Thymosin β4: actin-sequestering protein moonlights to repair injured tissues. Trends Mol Med. 2005;11(9):421-429. doi:10.1016/j.molmed.2005.07.004. PMID 16099219.
- Low TL, Hu SK, Goldstein AL. Complete amino acid sequence of bovine thymosin β4: a thymic hormone that induces terminal deoxynucleotidyl transferase activity in thymocyte populations. Proc Natl Acad Sci USA. 1981;78(2):1162-1166. doi:10.1073/pnas.78.2.1162. PMID 6940133.
- Safer D, Elzinga M, Nachmias VT. Thymosin β4 and Fx, an actin-sequestering peptide, are indistinguishable. J Biol Chem. 1991;266(7):4029-4032. PMID 1999398.
- Huff T, Müller CS, Otto AM, Netzker R, Hannappel E. β-Thymosins, small acidic peptides with multiple functions. Int J Biochem Cell Biol. 2001;33(3):205-220. doi:10.1016/s1357-2725(00)00087-x. PMID 11311852.
- Hannappel E. β-Thymosins. Ann N Y Acad Sci. 2007;1112:21-37. doi:10.1196/annals.1415.018. PMID 17468232.
- Philp D, Huff T, Gho YS, Hannappel E, Kleinman HK. The actin binding site on thymosin β4 promotes angiogenesis. FASEB J. 2003;17(14):2103-2105. doi:10.1096/fj.03-0121fje. PMID 14500546.
- Sosne G, Qiu P, Goldstein AL, Wheater M. Biological activities of thymosin β4 defined by active sites in short peptide sequences. FASEB J. 2010;24(7):2144-2151. doi:10.1096/fj.09-142307. PMID 20179146.
- Malinda KM, Sidhu GS, Mani H, et al. Thymosin β4 accelerates wound healing. J Invest Dermatol. 1999;113(3):364-368. doi:10.1046/j.1523-1747.1999.00708.x. PMID 10469335.
- Bock-Marquette I, Saxena A, White MD, DiMaio JM, Srivastava D. Thymosin β4 activates integrin-linked kinase and promotes cardiac cell migration, survival and cardiac repair. Nature. 2004;432(7016):466-472. doi:10.1038/nature03000. PMID 15565145.
- Smart N, Risebro CA, Melville AA, et al. Thymosin β4 induces adult epicardial progenitor mobilization and neovascularization. Nature. 2007;445(7124):177-182. doi:10.1038/nature05383. PMID 17108969.
- Ho JH, Chuang CH, Ho CY, Shih YR, Lee OK, Su Y. Internalization is essential for the antiapoptotic effects of exogenous thymosin β4 on human corneal epithelial cells. Invest Ophthalmol Vis Sci. 2007;48(1):27-33. doi:10.1167/iovs.06-0826. PMID 17197512.
- Cavasin MA. Therapeutic potential of thymosin-β4 and its derivative N-acetyl-seryl-aspartyl-lysyl-proline (Ac-SDKP) in cardiac healing after infarction. Am J Cardiovasc Drugs. 2006;6(5):305-311. doi:10.2165/00129784-200606050-00003. PMID 17083265.
- Crockford D, Turjman N, Allan C, Angel J. Thymosin β4: structure, function, and biological properties supporting current and future clinical applications. Ann N Y Acad Sci. 2010;1194:179-189. doi:10.1111/j.1749-6632.2010.05492.x. PMID 20536467.
- Ruff D, Crockford D, Girardi G, Zhang Y. A randomized, placebo-controlled, single and multiple dose study of intravenous thymosin β4 in healthy volunteers. Ann N Y Acad Sci. 2010;1194:223-229. doi:10.1111/j.1749-6632.2010.05474.x. PMID 20536472.
- Ho EN, Kwok WH, Lau MY, et al. Doping control analysis of TB-500, a synthetic version of an active region of thymosin β4, in equine urine and plasma by liquid chromatography-mass spectrometry. J Chromatogr A. 2012;1265:57-69. doi:10.1016/j.chroma.2012.09.043. PMID 23084823.
- Kwok WH, Ho EN, Lau MY, Leung GN, Wong AS, Wan TS. Doping control analysis of seven bioactive peptides in horse plasma by liquid chromatography-mass spectrometry. Anal Bioanal Chem. 2013;405(8):2595-2606. doi:10.1007/s00216-012-6697-9. PMID 23318763.
- Sikiric P, Seiwerth S, Rucman R, et al. Stable gastric pentadecapeptide BPC 157: novel therapy in gastrointestinal tract. Curr Pharm Des. 2011;17(16):1612-1632. doi:10.2174/138161211796196954. PMID 21548867.
- Manning MC, Chou DK, Murphy BM, Payne RW, Katayama DS. Stability of protein pharmaceuticals: an update. Pharm Res. 2010;27(4):544-575. doi:10.1007/s11095-009-0045-6. PMID 20143256.
Research Use Only Disclaimer. This article is an academic literature review of published research and public database identifiers. All compounds named are referenced strictly for research reference; not for human or veterinary use. Nothing here constitutes dosing guidance, preparation guidance, medical advice, or a health, performance or weight-related claim of any kind. Catalogue search strings are reproduced verbatim solely to resolve nomenclature; no vendor is assessed or endorsed.