The BPC-157 TB500 blend from BioLongevity Labs combines two synthetic research peptides, BPC-157 and TB-500 (Ac-LKKTETQ), in a single 10mg vial. Each vial holds 5mg of BPC-157 and 5mg of TB-500, supplied together as a white lyophilized powder for stable storage and handling. BPC-157 is a fifteen-residue peptide studied in angiogenic signaling and fibroblast migration research. TB-500 is a seven-residue acetylated peptide matching the actin-binding region of thymosin beta-4, characterized in actin regulation and cell migration studies in vitro.
≥99% Purity
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BPC-157 is a synthetic pentadecapeptide with the sequence GEPPPGKPADDAGLV. It is based on a sequence originally identified in a gastric juice protein known as body protection compound, and is produced here through controlled peptide synthesis.
TB-500 is a short synthetic peptide, Ac-Leu-Lys-Lys-Thr-Glu-Thr-Gln, that corresponds to residues 17 to 23 of thymosin beta-4 with an added N-terminal acetyl group. It is not the full 43-residue thymosin beta-4 protein, and the two should not be confused when comparing literature or COA data.
Researchers pair the two because each BPC-157 TB-500 peptide sits on a different side of the same cell-migration question. BPC-157 is studied through growth factor receptor and focal adhesion signaling, while the LKKTETQ motif is studied through its direct binding to monomeric actin. A 1:1 BPC TB500 blend lets both be handled from one vial in tissue-repair research models and in vitro assays.
Body Protection Compound-157, BPC 157, PL-14736, PLD-116
TB-500 Identity
N-acetylated LKKTETQ, a synthetic fragment matching residues 17 to 23 of thymosin beta-4 (not full-length thymosin beta-4)
TB-500 CAS Number
885340-08-9
TB-500 PubChem CID
62707662
TB-500 Molecular Formula
C₃₈H₆₈N₁₀O₁₄
TB-500 Molecular Weight
889.0 g/mol
TB-500 Exact Mass
888.492 Da
TB-500 Amino Acid Sequence
Ac-Leu-Lys-Lys-Thr-Glu-Thr-Gln-OH (Ac-LKKTETQ)
TB-500 Sequence Length
7 residues, N-terminal acetyl
TB-500 InChIKey
ADKDNDYYIZUVCZ-ZQNQAVPYSA-N
TB-500 UNII
QHK6Z47GTG
TB-500 Synonyms
TB500, Ac-LKKTETQ, N-acetyl-LKKTETQ, thymosin beta-4 fragment 17-23
Source
Synthetic (both peptides)
Purity
≥99% (HPLC)
Appearance
White lyophilized powder
Solubility
Soluble in sterile water
Storage
-20°C, protect from light
Storage and Handling
Store the lyophilized blend at -20°C, protected from light and moisture.
After reconstitution, store at 2°C to 8°C and use promptly.
Maintain aseptic handling to preserve compound integrity.
Lyophilized Format
This compound ships in lyophilized (freeze-dried) form. Freeze-drying supports long-term storage stability and preserves compound integrity. No fillers are added.
Research Use Disclaimer
BPC-157 TB-500 Blend is supplied for research use only. It is not a drug, food, cosmetic, or dietary supplement and has not been evaluated by the FDA. By purchasing, the buyer confirms the compound will be used solely for in vitro research.
Frequently Asked Questions
What Is the BPC-157 TB-500 Blend?
The BPC-157 TB-500 blend is a lyophilized research preparation that combines 5mg of BPC-157 and 5mg of TB-500 in one 10mg vial. Both peptides are made by synthesis and supplied for in vitro research use only.
Is the TB-500 in This Blend Full-Length Thymosin Beta-4?
No. The TB-500 in this blend is Ac-LKKTETQ (CAS 885340-08-9), a synthetic seven-residue peptide matching residues 17 to 23 of thymosin beta-4, not the 43-residue full-length protein.
What Are the Molecular Weights of BPC-157 and TB-500?
BPC-157 has a molecular weight of 1419.5 g/mol (C₆₂H₉₈N₁₆O₂₂), and TB-500 (Ac-LKKTETQ) has a molecular weight of 889.0 g/mol (C₃₈H₆₈N₁₀O₁₄).
How Should the BPC-157 TB-500 Blend Be Stored?
The lyophilized BPC-157 TB-500 blend should be kept at -20°C and protected from light and moisture. Once reconstituted, it is stored at 2°C to 8°C and used promptly.
How Is the Purity of the Blend Verified?
BioLongevity Labs specifies ≥99% purity (HPLC) for the BPC-157 TB-500 blend, confirmed by an independent third-party lab. The current Certificate of Analysis is published on the product page.
Research Overview
Laboratory work on BPC-157 centers on cell migration and angiogenic signaling. In rat tendon explant and fibroblast cultures, BPC-157 was associated with faster explant outgrowth, greater fibroblast migration in transwell assays, F-actin formation, and increased phosphorylation of FAK and paxillin [1].
In vascular endothelial cell culture, BPC-157 was associated with higher VEGFR2 expression, VEGFR2 internalization, activation of the VEGFR2-Akt-eNOS pathway, and increased tube formation, with the effect blocked by the endocytosis inhibitor dynasore [2].
The TB-500 side of the blend is defined by actin biology. Thymosin beta-4 was identified as an actin-sequestering peptide that forms a 1:1 complex with G-actin and inhibits its polymerization [3]. The LKKTETQ sequence at residues 17 to 23 is described as the central actin-binding domain of the protein [4].
The sections below look at how the short TB-500 motif behaves on its own in vitro, and how it has been characterized analytically.
The LKKTETQ Actin-Binding Motif in Vitro
Using full-length thymosin beta-4, proteolytic fragments, and synthetic peptides, one study found the seven-residue actin-binding motif was required for endothelial cell migration and aortic ring sprouting, with activity close to the full protein at about 50 nM [5].
Analytical Characterization of TB-500
An LC-MS method identified N-acetylated LKKTETQ as the key ingredient of TB-500 and confirmed the parent peptide and its metabolites at sub-nanogram levels [6].
A 2024 UHPLC-Orbitrap study quantified TB-500 and its metabolites in serum and enzyme incubations, naming Ac-LK as the main metabolite and Ac-LKK as a long-lived one. In fibroblast migration assays, activity was associated with the Ac-LKKTE metabolite rather than the parent peptide [7].
The research applications below summarize how each component of the blend is used in laboratory work.
Research Area
In Vitro Application
Angiogenic signaling
VEGFR2 expression, internalization, and VEGFR2-Akt-eNOS pathway activity in endothelial cell culture (BPC-157)
Actin regulation
G-actin binding and polymerization assays built around the LKKTETQ actin-binding motif (TB-500)
Cell migration
Transwell and spreading assays in tendon fibroblasts; endothelial migration and sprouting assays
Focal adhesion signaling
FAK and paxillin phosphorylation measured by Western blot (BPC-157)
Tissue-repair research models
Tendon explant outgrowth and fibroblast survival under oxidative stress (BPC-157)
Analytical chemistry
LC-MS identification of Ac-LKKTETQ and its metabolites Ac-LK, Ac-LKK, and Ac-LKKTE
References
Chang CH, Tsai WC, Lin MS, Hsu YH, Pang JH. (2011). The promoting effect of pentadecapeptide BPC 157 on tendon healing involves tendon outgrowth, cell survival, and cell migration. Journal of Applied Physiology. https://doi.org/10.1152/japplphysiol.00945.2010
Hsieh MJ, Liu HT, Wang CN, et al. (2017). Therapeutic potential of pro-angiogenic BPC157 is associated with VEGFR2 activation and up-regulation. Journal of Molecular Medicine. https://doi.org/10.1007/s00109-016-1488-y
Safer D, Elzinga M, Nachmias VT. (1991). Thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable. The Journal of Biological Chemistry. https://pubmed.ncbi.nlm.nih.gov/1999398/
Sosne G, Qiu P, Goldstein AL, Wheater M. (2010). Biological activities of thymosin beta4 defined by active sites in short peptide sequences. The FASEB Journal. https://doi.org/10.1096/fj.09-142307
Philp D, Huff T, Gho YS, Hannappel E, Kleinman HK. (2003). The actin binding site on thymosin beta4 promotes angiogenesis. The FASEB Journal. https://doi.org/10.1096/fj.03-0121fje
Ho EN, Kwok WH, Lau MY, et al. (2012). 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. Journal of Chromatography A. https://doi.org/10.1016/j.chroma.2012.09.043
Rahaman KA, Muresan AR, Min H, et al. (2024). Simultaneous quantification of TB-500 and its metabolites in in-vitro experiments and rats by UHPLC-Q-Exactive orbitrap MS/MS and their screening by wound healing activities in-vitro. Journal of Chromatography B. https://doi.org/10.1016/j.jchromb.2024.124033
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Scientifically reviewed by Dr. Ky H. Le, MD. Dr. Le is a board-certified family medicine physician with over 20 years of clinical experience. Dr. Le validates the scientific accuracy of all technical content and research citations.
Disclaimer: For Research Purposes Only
This content is provided strictly for research purposes and does not constitute an endorsement or recommendation for the non-laboratory application or improper handling of peptides designed for research. The information, including discussions about specific peptides and their researched benefits, is presented for informational purposes only and must not be construed as health, clinical, or legal guidance, nor an encouragement for non-research use. Peptides described here are solely for use in structured scientific study by authorized individuals. We advise consulting with research experts, medical practitioners, or legal counsel prior to any decisions about obtaining or utilizing these peptides. The expectation of responsible, ethical utilization of this information for legitimate investigative and scholarly objectives is paramount. This notice is dynamic and governs all provided content on research peptides.
