TB-500 (10 Vials)

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For Laboratory Research Only: This listing is intended strictly for qualified researchers conducting laboratory work. Completing a purchase confirms you meet this criteria and will not use the product for personal or human consumption.
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Description

TB-500 (Thymosin Beta-4 Fragment)

TB-500 is a synthetic research peptide matching the active actin-binding segment (LKKTETQ) of Thymosin Beta-4 (Tβ4), a naturally occurring protein present in nearly all mammalian cells, known for its involvement in tissue repair and cell movement.

Mechanism of Action

  • TB-500’s primary activity is binding to actin, a structural protein central to cell shape, motility, and division. Through this interaction, the peptide influences how cells migrate toward sites of injury
  • Research indicates it supports new blood vessel formation, aids collagen deposition, and helps moderate inflammation in preclinical wound repair models (Goldstein et al., 2012)
  • Preclinical studies also show a reduction in scar tissue formation, linked to fewer myofibroblasts present at the wound site (Goldstein et al., 2012)

Key Research Findings

  • In rodent models, both topical and systemic application of the parent Tβ4 sequence increased wound re-epithelialisation by as much as 61% relative to controls, with the actin-binding fragment alone showing comparable repair activity (Philp et al., 2003)
  • Rahaman et al. (2024) found that some of TB-500’s wound-healing activity in fibroblast models may trace back to its metabolite Ac-LKKTE, underscoring why metabolite profiling remains a relevant part of ongoing research
  • Esposito et al. (2012) confirmed and characterised the structural identity of TB-500 (Ac-LKKTETQ) using high-resolution mass spectrometry

For research use only. Not intended for use in humans or animals.

References

Esposito, S., Deventer, M., Van Thuyne, W., Delbeke, F. T., & Van Eenoo, P. (2012). https://pubmed.ncbi.nlm.nih.gov/22962027/
Goldstein, A. L., Hannappel, E., Sosne, G., & Kleinman, H. K. (2012). https://pubmed.ncbi.nlm.nih.gov/22074294/
Philp, D., Badamchian, M., Scheremeta, B., Nguyen, M., Goldstein, A. L., & Kleinman, H. K. (2003). https://pubmed.ncbi.nlm.nih.gov/12581422/
Rahaman, K. A., Muresan, A. R., Min, H., Son, J., Kang, M. J., & Kwon, O. S. (2024). https://www.sciencedirect.com/science/article/pii/S1570023224000412

Additional information

Size

5mg/vial

What is a peptide, exactly?

Peptides are short chains of amino acids, smaller than proteins, that function as signalling molecules within biological systems. They're involved in processes such as tissue repair, immune activity, and communication between cells.

What role do peptides play in research?

Peptides are studied for how selectively they bind to receptors and influence specific cellular pathways. That precision makes them a valuable tool in laboratory settings for investigating how biological systems function at a molecular level.

What are my payment options?

Card payment, UK bank transfer, and cryptocurrency (Bitcoin and Ethereum) are all accepted.

How do I store this product correctly?

This product ships lyophilised (freeze-dried) to remain stable throughout transit and storage. Keep it cool, dry, and shielded from direct light before use, refrigerating if holding it longer term. Once reconstituted, refrigerate immediately and handle with standard sterile technique to preserve integrity.

What are your shipping timeframes?

Delivery is UK-only. Orders placed before 2pm on a business day go out same-day; anything later, or placed on a weekend, ships the next business day. Most orders arrive within 48 hours of dispatch, with tracking sent directly to you. Orders over £200 ship free automatically.

What's your policy on returns?

As a research product, this item isn't eligible for standard returns. If it arrives damaged or you received the wrong item, reach out within 48 hours and we'll get it resolved.

How is purity confirmed for this product?

Every batch is independently tested in a laboratory before listing, confirming it meets research-grade purity standards. A Certificate of Analysis is available for this product.

TB-500 (Thymosin Beta-4 Fragment)

TB-500 is a synthetic research peptide matching the active actin-binding segment (LKKTETQ) of Thymosin Beta-4 (Tβ4), a naturally occurring protein present in nearly all mammalian cells, known for its involvement in tissue repair and cell movement.

Mechanism of Action

  • TB-500’s primary activity is binding to actin, a structural protein central to cell shape, motility, and division. Through this interaction, the peptide influences how cells migrate toward sites of injury
  • Research indicates it supports new blood vessel formation, aids collagen deposition, and helps moderate inflammation in preclinical wound repair models (Goldstein et al., 2012)
  • Preclinical studies also show a reduction in scar tissue formation, linked to fewer myofibroblasts present at the wound site (Goldstein et al., 2012)

Key Research Findings

  • In rodent models, both topical and systemic application of the parent Tβ4 sequence increased wound re-epithelialisation by as much as 61% relative to controls, with the actin-binding fragment alone showing comparable repair activity (Philp et al., 2003)
  • Rahaman et al. (2024) found that some of TB-500’s wound-healing activity in fibroblast models may trace back to its metabolite Ac-LKKTE, underscoring why metabolite profiling remains a relevant part of ongoing research
  • Esposito et al. (2012) confirmed and characterised the structural identity of TB-500 (Ac-LKKTETQ) using high-resolution mass spectrometry

For research use only. Not intended for use in humans or animals.

References

Esposito, S., Deventer, M., Van Thuyne, W., Delbeke, F. T., & Van Eenoo, P. (2012). https://pubmed.ncbi.nlm.nih.gov/22962027/
Goldstein, A. L., Hannappel, E., Sosne, G., & Kleinman, H. K. (2012). https://pubmed.ncbi.nlm.nih.gov/22074294/
Philp, D., Badamchian, M., Scheremeta, B., Nguyen, M., Goldstein, A. L., & Kleinman, H. K. (2003). https://pubmed.ncbi.nlm.nih.gov/12581422/
Rahaman, K. A., Muresan, A. R., Min, H., Son, J., Kang, M. J., & Kwon, O. S. (2024). https://www.sciencedirect.com/science/article/pii/S1570023224000412