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TB-500 is a synthetic peptide fragment corresponding to the active region of Thymosin Beta-4 (Tβ4), a naturally occurring 43-amino-acid protein involved in cell motility, differentiation, and survival. CAS number: 77591-33-4. It is supplied as a lyophilized powder for in vitro and preclinical research.
Thymosin Beta-4 was first isolated from the thymus gland in the 1960s and has since been identified in virtually all mammalian cell types. The synthetic fragment TB-500 replicates the actin-binding domain of the full protein, which is central to its biological activity in research models.
The primary documented mechanism of TB-500 involves its interaction with the actin cytoskeleton. TB-500 binds to monomeric G-actin, preventing premature polymerization into F-actin filaments. This sequestration creates a pool of available actin monomers that can be rapidly deployed for cytoskeletal reorganization — a process essential for cell migration, wound closure, and tissue remodeling.
In both in vitro scratch assays and in vivo wound models, TB-500 has been observed to promote directional cell migration. The mechanism appears related to its effects on actin dynamics: by maintaining a readily available pool of G-actin, cells at wound edges can rapidly extend lamellipodia and migrate into the wound space.
Several published studies have reported anti-inflammatory effects associated with TB-500 administration in preclinical models. In rodent cardiac injury models, TB-500 treatment was associated with reduced inflammatory cell infiltration and decreased expression of pro-inflammatory cytokines relative to controls. The mechanism underlying these observations has not been fully elucidated.
The most established research application for TB-500 involves wound healing models. Multiple studies have demonstrated accelerated wound closure in rodent models, with increased angiogenesis (new blood vessel formation) at wound sites. These effects have been attributed to both the actin-related migration enhancement and upregulation of vascular endothelial growth factor.
Published work in mouse models of myocardial infarction has shown that TB-500 administration post-injury was associated with reduced scar size and improved cardiac function metrics compared to untreated controls. These studies have generated significant interest in Tβ4 biology, though translation to human cardiac research remains in early stages.
TB-500 has been studied in corneal wound healing models, where its effects on epithelial cell migration are particularly relevant. This research has progressed further toward clinical investigation than most other applications, with the full-length Tβ4 protein having entered clinical trials for ophthalmic indications under the name RGN-259.
As with most peptide research, the TB-500 literature is predominantly preclinical. Rodent and cell culture models make up the vast majority of published data. The translation gap between these models and any human application remains significant.
Researchers should also note that TB-500 (the synthetic fragment) and full-length Thymosin Beta-4 are not identical in all contexts. While they share the actin-binding domain, the full protein contains additional functional regions that may contribute to biological effects observed in some studies.
CAS Number: 77591-33-4. Form: Lyophilized powder. Purity: ≥98% (HPLC). Storage: -20°C. Available strength: 10 mg.
All TB-500 from Vial & Error Labs includes a lot-specific COA and GHS-compliant SDS. For research use only.
A Certificate of Analysis (COA) is an analytical document issued by the manufacturer or an independent testing laboratory that reports the results of quality testing performed on a specific production lot of a compound. It serves as the primary quality assurance document for research reagents and is the closest thing to a “receipt of quality” that exists in the supply chain.
A COA is not a marketing document. It is not a certificate of “goodness” or a general quality claim. It documents specific, measurable test results for a specific batch. Understanding this distinction is the first step in reading one correctly.
This section should include the compound name, CAS number, molecular formula, molecular weight, and lot/batch number. The lot number is critical — it ties the test results to the specific batch you received. If the lot number on your vial does not match the lot number on the COA, the document does not apply to your product.
The most important result on most peptide COAs is the HPLC purity value. This represents the percentage of the total material that is the target compound, as measured by high-performance liquid chromatography. A result of ≥98% means that at least 98% of the detected material is the compound of interest, with ≤2% being other species (synthesis impurities, degradation products, or related substances).
Look for the testing method description: reverse-phase HPLC is standard for peptides. The COA should specify the column type, mobile phase, and detection wavelength — though not all manufacturers include this level of detail.
A purity number alone does not confirm identity — it only tells you that the material is pure, not that it is what it claims to be. Identity confirmation typically comes from mass spectrometry (MS), which verifies the molecular weight matches the expected value. Look for an MS result showing the observed mass matches the theoretical mass within acceptable tolerance.
The COA may describe the physical appearance (e.g., “white to off-white lyophilized powder”), solubility, and pH. These are less quantitative than HPLC and MS but provide baseline expectations for what you should see when you open the vial.
Missing lot number or batch number (makes the document unverifiable). No HPLC result or a purity result stated as a range without a specific measured value. No mass spectrometry confirmation of identity. Generic or template-style COAs that do not appear to reflect actual testing. COAs dated significantly before or after the labeled production date. Results that exactly match the specification with no variance (e.g., “Purity: 99.0%” every time — real analytical testing produces variable results).
A trustworthy COA includes a specific lot number matching your product, a measured HPLC purity value (not a range), mass spectrometry confirmation, a specific test date, identification of the testing laboratory or manufacturer, and method details or references.
Every compound from Vial & Error Labs ships with a lot-specific COA from the manufacturer. Our COA Library provides digital access to these documents by SKU or lot number. If you have questions about a specific COA, contact us. For research use only.
A Certificate of Analysis (COA) is an analytical document issued by the manufacturer or an independent testing laboratory that reports the results of quality testing performed on a specific production lot of a compound. It serves as the primary quality assurance document for research reagents and is the closest thing to a “receipt of quality” that exists in the supply chain.
A COA is not a marketing document. It is not a certificate of “goodness” or a general quality claim. It documents specific, measurable test results for a specific batch. Understanding this distinction is the first step in reading one correctly.
This section should include the compound name, CAS number, molecular formula, molecular weight, and lot/batch number. The lot number is critical — it ties the test results to the specific batch you received. If the lot number on your vial does not match the lot number on the COA, the document does not apply to your product.
The most important result on most peptide COAs is the HPLC purity value. This represents the percentage of the total material that is the target compound, as measured by high-performance liquid chromatography. A result of ≥98% means that at least 98% of the detected material is the compound of interest, with ≤2% being other species (synthesis impurities, degradation products, or related substances).
Look for the testing method description: reverse-phase HPLC is standard for peptides. The COA should specify the column type, mobile phase, and detection wavelength — though not all manufacturers include this level of detail.
A purity number alone does not confirm identity — it only tells you that the material is pure, not that it is what it claims to be. Identity confirmation typically comes from mass spectrometry (MS), which verifies the molecular weight matches the expected value. Look for an MS result showing the observed mass matches the theoretical mass within acceptable tolerance.
Appearance and Physical Properties
The COA may describe the physical appearance (e.g., “white to off-white lyophilized powder”), solubility, and pH. These are less quantitative than HPLC and MS but provide baseline expectations for what you should see when you open the vial.
Missing lot number or batch number (makes the document unverifiable). No HPLC result or a purity result stated as a range without a specific measured value. No mass spectrometry confirmation of identity. Generic or template-style COAs that do not appear to reflect actual testing. COAs dated significantly before or after the labeled production date. Results that exactly match the specification with no variance (e.g., “Purity: 99.0%” every time — real analytical testing produces variable results).
A trustworthy COA includes a specific lot number matching your product, a measured HPLC purity value (not a range), mass spectrometry confirmation, a specific test date, identification of the testing laboratory or manufacturer, and method details or references. Every compound from Vial & Error Labs ships with a lot-specific COA from the manufacturer. Our COA Library provides digital access to these documents by SKU or lot number. If you have questions about a specific COA, contact us. For research use only.
BPC-157 and TB-500 are arguably the two most discussed peptides in tissue repair research, and they are frequently mentioned together — sometimes interchangeably. This is a mistake. While both have been studied in wound healing and tissue repair contexts, they operate through fundamentally different mechanisms, target different cellular processes, and have distinct research profiles.
Understanding these differences matters for designing research protocols and selecting appropriate compounds for specific models.
BPC-157 (CAS 1628202-19-6) operates primarily through nitric oxide system modulation and growth factor upregulation. Its documented effects include VEGF, FGF, and HGF upregulation, interaction with the FAK-paxillin signaling pathway, and modulation of nitric oxide synthase activity. The compound’s effects are largely mediated through extracellular signaling cascades that influence tissue repair from the outside in.
TB-500 (CAS 77591-33-4) works through a fundamentally intracellular mechanism — binding G-actin monomers to regulate cytoskeletal dynamics. This affects cell migration, lamellipodia formation, and the physical machinery cells use to move into wound spaces. TB-500’s effects are primarily about enabling cellular movement and reorganization at the structural level.
Both peptides have been studied in soft tissue repair, wound healing, and musculoskeletal injury models. In these overlapping contexts, they appear to contribute to healing through complementary rather than redundant pathways — which is why combinatorial research (using both simultaneously) has generated interest.
BPC-157 has a substantial body of gastrointestinal research that TB-500 does not share. GI models including ulcers, inflammatory bowel disease, and intestinal anastomosis healing represent a major application area unique to BPC-157.
Conversely, TB-500 has a stronger research profile in cardiac injury models and corneal healing. The actin-based mechanism is particularly relevant to tissues where cell migration is the rate-limiting step in repair, such as corneal epithelium.
Both compounds are supplied as lyophilized powders requiring reconstitution. BPC-157 is typically available in 5 mg vials, while TB-500 is commonly supplied at 10 mg. Both require storage at -20°C and standard peptide handling protocols.
From a stability perspective, both peptides are relatively stable in lyophilized form but should be protected from moisture and light. Once reconstituted, standard peptide degradation considerations apply — avoid repeated freeze-thaw cycles and use within a reasonable timeframe.
The complementary mechanisms of BPC-157 and TB-500 have led to interest in combined-use research protocols. Vial & Error Labs carries both compounds individually (BPC-157 5 mg, TB-500 10 mg) as well as a pre-compounded BPC-157 + TB-500 blend (10 mg) for researchers investigating combinatorial approaches.
Whether combination use offers advantages over individual compounds is a research question, not a marketing claim. The mechanistic rationale for complementary effects exists, but controlled comparative studies are limited.
All compounds ship with lot-specific COA and SDS. For research use only.