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TB-500 10mg

$71.88

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A synthetic fragment of thymosin beta-4, the principal actin-sequestering protein, designed for investigating cellular migration, anti-inflammatory signaling, and tissue remodeling pathways. For research use only.

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Orders placed today are expected to arrive Apr 18 - Apr 20
Purchased Apr 16
Processing Apr 16 - Apr 17
Delivered Apr 18 - Apr 20
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Buyer Protection & Quality Assurance

Every order is backed by full reship or refund coverage, including international shipments. All products are produced under documented lab procedures and ship with batch-verified COAs — what’s on the label is exactly what’s in the vial.

Description

This 43-amino acid peptide represents the active domain of thymosin beta-4 and serves as a versatile research tool for studying G-actin dynamics, cell motility, and extracellular matrix remodeling. Its well-characterized mechanism of action provides a reliable platform for controlled tissue repair investigations. For research use only.

  • Actin Polymerization & Cell Migration: Investigated for G-actin sequestration and the promotion of lamellipodial extension in keratinocyte and endothelial cell migration assays.
  • Anti-Inflammatory Signaling: Studied for the downregulation of pro-inflammatory cytokines including IL-1β, TNF-α, and NF-κB pathway components in acute inflammation models.
  • Cardiac & Vascular Remodeling: Explored for its role in epicardial progenitor cell activation and neovascularization in ischemic tissue research models.
  • Actin Polymerization & Cell Migration: Investigated for G-actin sequestration and the promotion of lamellipodial extension in keratinocyte and endothelial cell migration assays.
  • Anti-Inflammatory Signaling: Studied for the downregulation of pro-inflammatory cytokines including IL-1β, TNF-α, and NF-κB pathway components in acute inflammation models.
  • Cardiac & Vascular Remodeling: Explored for its role in epicardial progenitor cell activation and neovascularization in ischemic tissue research models.

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Always quality-tested, verified with third-party COAs

Every Synthro Lab batch is independently screened for identity, purity, and endotoxins before it ever leaves our facility. No lot is released until it meets our research-grade threshold and clears third-party verification — documented in a COA that ships with every order.

The result is simple: no guesswork, no surprises — just material you can build your research on.

Identity Test

Passed

Verifies the peptide’s sequence and structure so the correct compound is present in each vial.

Purity Test

Passed

Measures purity and concentration to confirm ≥99% purity on qualifying batches.

Sterility Test

Passed

Screens for bacteria, fungi, and other microorganisms to verify sterile handling.

Endotoxicity

Passed

Tests for lipopolysaccharides (LPS) to ensure endotoxin levels stay within research limits.

Commonly asked Questions by Researchers

Everything you need to know before you order — batch verification, COA documentation, storage conditions, and handling guidelines, all in one place.

Each Synthro Lab batch goes through HPLC and mass spectrometry analysis to confirm identity and purity — nothing ships until it clears our verification process.

Absolutely. Every product ships with a batch-specific COA that includes identity confirmation, purity data, and endotoxin results for full research traceability.

All peptides arrive as lyophilized powder in individually sealed vials, clearly labeled with the peptide name, lot number, and quantity.

We target ≥98% purity by HPLC across our entire catalog. The exact value for each batch is documented on the COA — no approximations.

Unopened vials should be kept sealed, away from light and humidity, and stored refrigerated or frozen per the guidelines listed on the COA.

Reconstituted peptides should be aliquoted and stored under refrigerated or frozen conditions to preserve stability and reduce the number of freeze–thaw cycles.

It depends on the peptide, but lyophilized vials stored correctly are stable long-term. Check the COA for batch-specific stability and expiry information.

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