TB-500 (10mg)
TB-500 (10mg)
Couldn't load pickup availability
TB-500 (10mg)
TB-500 (Thymosin Beta-4 Fragment) is a synthetic peptide composed of 43 amino acids and derived from the active sequence of the naturally occurring protein Thymosin Beta-4. It is designed to replicate specific regions of the parent molecule, most notably the LKKTETQ sequence (residues 16–24), which has been studied for its role in actin binding. In experimental settings, TB-500 has been used to investigate actin sequestration, the regulation of cytoskeletal dynamics, and the potential influence on cellular motility and structural adaptation. With its stability and high purity, TB-500 serves as a valuable compound for laboratory research into peptide–protein interactions and cellular processes.
Disclaimer: This material is supplied for laboratory research use only. It is not intended for human consumption, therapeutic, or diagnostic applications.
- Fast Shipping
99% Purity
- Made in USA
What is TB-500?
TB-500 is a synthetic peptide fragment derived from thymosin beta-4 (Tβ4), specifically corresponding to the 17-23 amino acid sequence (LKKTETQ) within the actin-binding domain. This research compound has been studied for its interactions with cellular migration pathways, angiogenic signaling mechanisms, and tissue remodeling processes. Scientific investigations have documented the peptide's molecular interactions with actin cytoskeleton dynamics and wound healing systems in laboratory environments, making it valuable for studying tissue repair and regeneration in experimental research applications.
Chemical Structure of TB-500
- Full-length Thymosin Beta-4 (TB4): 43-amino acid peptide with molecular formula C₂₁₂H₃₅₀N₅₆O₇₈S and molecular weight of approximately 4,960 Da (PubChem CID: 16132341)
- TB-500 Active Fragment: 7-amino acid sequence Leu-Lys-Lys-Thr-Glu-Thr-Gln (LKKTETQ), corresponding to positions 17-23, with molecular formula C₃₈H₆₈N₁₀O₁₄ and molecular weight of approximately 889 Da (PubChem CID: 62707662)
- Active Domain: Actin-binding region with enhanced stability and tissue penetration characteristics for laboratory research applications
Research and Clinical Studies on TB-500
1. Inflammation Research Studies: Laboratory investigations have examined TB-500's interactions with microRNA-146a pathways and inflammatory cytokine signaling, documenting its influence on IRAK1 and TRAF6 protein expression in anti-inflammatory pathway studies.
2. Wound Healing Research Models: Scientific studies have investigated TB-500's effects on re-epithelialization and collagen deposition mechanisms, documenting interactions with angiogenesis pathways in acute and chronic wound models across various experimental conditions.
3. Cardiovascular Research Applications: Experimental investigations have explored TB-500's interactions with cardiac cell regeneration and pulmonary hypertension models, documenting influence on Notch3-Col 3A-CTGF gene expression and kinase signaling in cardiac tissue research.
4. Angiogenesis & Vascular Research: Laboratory studies have investigated TB-500's role in endothelial cell migration and VEGF expression, examining interactions with Notch/NF-κB pathways and angiopoietin-2 signaling in vascular development studies.
5. Cellular Migration & Cytoskeletal Research: Scientific investigations have documented TB-500's interactions with actin polymerization pathways and cellular motility, exploring influence on cytoskeletal organization and keratinocyte migration in experimental applications.
6. Tissue Regeneration Studies: Research has examined TB-500's effects on hair follicle activation, corneal healing, and neuroregeneration pathways, documenting anti-apoptotic mechanisms and survival kinase interactions in tissue regeneration models.
Citations
4. Malinda, K. M., et al. "Thymosin β4 Accelerates Wound Healing." Journal of Investigative Dermatology, vol. 113, no. 3, pp. 364–368, 1999.
5. Wei, C., et al. "Thymosin Beta 4 protects mice from monocrotaline-induced pulmonary hypertension and right ventricular hypertrophy." PLoS One, vol. 9, no. 11, e110598, 2014.