Description
Thymosin Beta-4 (TB-500) Technical Data Sheet
Compound Identification
Systematic Name: Thymosin β4
Sequence: Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser
Molecular Formula: C212H350N56O78S
Molecular Weight: 4963.4 g/mol
CAS Number: 77591-33-4
Peptide Type: 43-amino acid peptide, N-terminally acetylated
Chemical Properties
Appearance: White to off-white lyophilized powder
Solubility: Soluble in water and physiological buffers
Stability: Stable as lyophilized powder at -20°C for 24 months
pH Range: 6.0-8.0
Isoelectric Point: ~5.1
Storage Requirements: Lyophilized at -20°C; reconstituted at 2-8°C for up to 14 days
Origin and Background
Thymosin β4 (Tβ4) is a naturally occurring peptide first isolated from thymus tissue in the 1960s. It is one of the most abundant peptides in mammalian cells and plays important roles in tissue repair, wound healing, and cellular migration. The peptide is highly conserved across species, with identical sequences in humans, rats, and mice.
Proposed Mechanisms (Based on Preclinical Research)
Actin Sequestration: Primary mechanism involves binding G-actin monomers, regulating actin polymerization
Cell Migration: Promotes cell migration through actin cytoskeleton remodeling
Angiogenesis Modulation: Stimulates endothelial cell differentiation and new blood vessel formation
Anti-inflammatory Effects: Modulates inflammatory cytokine production and reduces inflammatory cell infiltration
Extracellular Matrix Regulation: Influences production and deposition of collagen and other matrix proteins
Wound Healing Pathways: Promotes keratinocyte and fibroblast migration to wound sites
Research Applications in Animal Models
Tissue Repair and Wound Healing
Extensively studied in rodent models of:
- Dermal wound healing (typical dose: 1-10 mg/kg, IP or SC)
- Tendon and ligament injuries
- Muscle damage and regeneration
- Corneal injury models
Cardiovascular Research
Investigated in models of:
- Myocardial infarction (doses: 0.5-6 mg/kg)
- Cardiac remodeling
- Vascular injury and atherosclerosis
Neurological Research
Studies in models of:
- Stroke and ischemic brain injury
- Traumatic brain injury
- Spinal cord injury
- Peripheral nerve damage
Inflammatory Conditions
Animal research examining effects in models of inflammatory bowel disease, arthritis, and sepsis.
Clinical Research Status
Regulatory Status: Not approved for human therapeutic use by FDA or EMA
Clinical Investigations: Limited Phase I/II trials for:
- Pressure ulcers
- Venous stasis ulcers
- Dry eye syndrome
- Acute myocardial infarction
Development Compounds: Synthetic analogs under investigation (e.g., RGN-352)
Current Status: Primarily research-use compound; some veterinary applications investigated
In Vitro Research Parameters
Cell culture studies commonly examine:
- Concentration range: 1-100 μg/mL (typical: 10-50 μg/mL)
- Cell types: Fibroblasts, endothelial cells, keratinocytes, cardiomyocytes, neural cells
- Assays: Cell migration (scratch/transwell), actin polymerization, angiogenesis (tube formation), proliferation
Research Limitations and Considerations
Actin Binding Ubiquity: Primary mechanism (actin sequestration) is fundamental to all cells; specific effects may be context-dependent
Dosing Variability: Published studies show wide dose ranges with limited systematic dose-response data
Route Sensitivity: Effects may vary significantly by administration route
Half-life: Relatively short half-life (hours) may require frequent dosing or continuous infusion in some models
Clinical Translation: Limited human clinical data; most evidence from animal models
Stability: Susceptible to oxidation of methionine residues; handle appropriately
Reconstitution Protocol for Laboratory Use
- Equilibrate vial to room temperature
- Add sterile water or saline slowly
- Allow to stand 3-5 minutes
- Gently swirl to dissolve (avoid vigorous shaking)
- Visually inspect for complete dissolution
- Aliquot if needed to avoid repeated freeze-thaw
Quality Control Specifications
Purity: ≥95% by RP-HPLC
Peptide Content: ≥80% by amino acid analysis
Endotoxin Level: <1.0 EU/mg
Water Content: <5% (Karl Fischer)
N-terminal Acetylation: Confirmed by mass spectrometry
Appearance: White powder, clear colorless solution when reconstituted
Safety Considerations for Laboratory Handling
- Standard peptide handling procedures
- Use appropriate PPE (gloves, lab coat, eye protection)
- Avoid aerosol generation
- Work in adequately ventilated area
- Follow institutional protocols for peptide handling
- Dispose per biological waste guidelines
Selected References from Primary Literature
- Goldstein, A.L., et al. (2005). Thymosin β4: a multi-functional regenerative peptide. Basic properties and clinical applications. Expert Opinion on Biological Therapy, 5(1), 37-48.
- Bock-Marquette, I., et al. (2004). Thymosin β4 activates integrin-linked kinase and promotes cardiac cell migration, survival and cardiac repair. Nature, 432(7016), 466-472.
- Philp, D., et al. (2003). Thymosin β4 promotes matrix metalloproteinase expression during wound healing in diabetic rats. Journal of Cellular Physiology, 197(3),
-406.
- Smart, N., et al. (2007). Thymosin β4 induces adult epicardial progenitor mobilization and neovascularization. Nature, 445(7124), 177-182.
- Sosne, G., et al. (2002). Thymosin beta 4 promotes corneal wound healing and decreases inflammation in vivo following alkali injury. Experimental Eye Research, 74(2), 293-299.
Research Use Statement
For laboratory research in vitro and in vivo animal models under appropriate institutional approval. Not approved for human or veterinary therapeutic applications. Researchers must comply with all applicable regulations and institutional guidelines.
Globally sourced Thymosin Beta 4 (TB500) in 5mg concentration, researched for its role in tissue repair and recovery. For research use only.




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