Tissue repair & recovery research
TB-500 (Ac-LKKTETQ) (TB-500): Research Overview
The seven-amino-acid active site of thymosin beta-4, studied in wound healing research.
Also known as Ac-LKKTETQ · thymosin beta-4 fragment 17-23 · TB-500
What is TB-500?
TB-500 (Ac-LKKTETQ) is a synthetic derivative of thymosin beta-4 consisting of the N-terminal acetylated 17-23 amino acid fragment. This sequence represents the active site within thymosin beta-4 responsible for actin binding, cell migration, and wound healing.
What is TB-500 researched for?
- Promotes dermal wound healing through the active LKKTETQ sequence.
- Supports tissue repair comparable to full thymosin beta-4 in research.
- Promotes keratinocyte migration and collagen deposition.
- Promotes endothelial cell differentiation and new blood vessel formation.
- Decreases inflammatory responses in damaged tissues.
How does TB-500 work?
TB-500 contains the LKKTETQ sequence which is the actin-binding motif of full-length thymosin beta-4. This fragment shares many properties of the parent protein regarding cell proliferation, differentiation, and migration. It promotes angiogenesis by upregulating VEGF expression and enhancing endothelial cell sprouting.
References
Synthesis and Characterization of N-terminal Acetylated 17-23 Fragment of Thymosin Beta-4 Drug Testing and Analysis
2012
TB-500 contains Ac-LKKTETQ, the active site responsible for actin binding and wound healing.
Doping Control Analysis of TB-500
Journal of Chromatography B · 2012
TB-500 is a synthetic version of the active region of thymosin beta-4.
TB-500 Metabolism and Wound Healing Journal of
Chromatography B · 2024
TB-500 undergoes serial cleavage at C-terminus; acetylation protects N-terminus.
Investigation of TB-500
Metabolism WADA · 2018
Characterized human metabolism of TB-500 using liver microsomes and S9 fraction.
Common questions
Is TB-500 fragment (Ac-LKKTETQ) the same as full TB-500?
TB-500 fragment is the active 7-amino-acid sequence (LKKTETQ) of the larger 43-amino-acid thymosin beta-4. Both promote wound healing and cell migration, but the fragment is more stable due to N-terminal acetylation and may be more cost-effective while retaining core regenerative properties.