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| 21+ | 20% | €51.98 |
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BPC-157 & TB-500 is a dual-peptide research formulation that combines two widely studied research peptides into a single compound. Sometimes referred to as the Wolverine Blend, this 5/5 mg BPC-157 & TB-500 formulation contains equal amounts of BPC-157 and TB-500 and enables researchers to investigate the complementary biological properties of both peptides within the same experimental model.
Researchers throughout the European Union can buy BPC-157 & TB-500 from Crystal Peptides as a high-purity research formulation, tested by accredited third-party labs for purity and quality. Certificates of Analysis are provided by the testing facility and are available on the product page, helping researchers confirm peptide identity, purity, and suitability for research. BPC157 & TB-500 Blend is supplied exclusively for research purposes and is not authorised as a medicinal product by the European Medicines Agency (EMA) or any other major medicines regulator.
Although frequently studied together, BPC-157 and TB-500 are structurally unrelated peptides with distinct biological characteristics. BPC-157 is a synthetic pentadecapeptide derived from a naturally occurring gastric protein fragment and has been investigated for its interactions with growth factor signalling, angiogenesis, nitric oxide pathways, and connective tissue biology.
On other hand, TB-500 is a synthetic peptide corresponding to the biologically active region of thymosin beta-4 and has primarily been studied for its role in actin regulation, cell migration, cytoskeletal organisation, and tissue remodelling.
Because these biological pathways are complementary rather than identical, researchers often investigate both peptides together in experimental models of musculoskeletal tissues, connective tissue biology, wound repair, vascular adaptation, and broader regenerative processes. The blend is supplied as a co-lyophilised laboratory reagent, with each peptide retaining its individual molecular identity and pharmacological characteristics following reconstitution.
Properties | BPC-157 | TB-500 |
|---|---|---|
Name and synonyms | BPC-157, Body Protection Compound-157, PL 14736 | TB-500, Thymosin Beta-4 Fragment |
PubChem CID | 9941957 | 62707662 |
CAS number | 137525-51-0 | 885340-08-9 |
Molecular formula | C62H98N16O22 | C38H68N10O14 |
Molecular weight | 1419.5 g/mol | 4963.4 g/mol |
Peptide length | 15 amino acids | 43 amino acids |
Compound class | Synthetic gastric pentadecapeptide | Synthetic thymosin beta-4 analogue |
Primary research focus | Angiogenesis, connective tissue biology, nitric oxide signalling | Cell migration, actin dynamics, cytoskeletal organisation |
Mechanism | Under investigation; multiple signalling pathways proposed | Actin-binding peptide involved in cytoskeletal remodelling |
Physical form | Lyophilised powder | Lyophilised powder |
Solubility | Bacteriostatic or sterile water | Bacteriostatic or sterile water |
Purity | Please see COA | Please see COA |
Supplied as | Co-lyophilised blend | Co-lyophilised blend |
The BPC-157 & TB-500 blend contains two independently characterised peptides supplied in equal proportions within a single co-lyophilised vial. Each peptide retains its own molecular identity, physicochemical properties, and proposed biological mechanisms following reconstitution.
Although supplied together for convenience, BPC-157 and TB-500 should be regarded as complementary research compounds rather than a single molecular entity. Their individual molecular formulas, molecular weights, and registry information therefore remain unchanged within the blend.
Each of the peptides in the BPC-157 & TB-500 blend has been independently characterised and investigated across different areas of regenerative biology. While the published literature has primarily evaluated BPC-157 as an individual research compound, its reported effects on connective tissue physiology, angiogenesis, and cellular signalling have made it one of the most widely studied regenerative peptides in preclinical research.
Using cultured rat Achilles tendon explants, Chang and colleagues demonstrated that BPC-157 accelerated tendon outgrowth, enhanced fibroblast migration, and improved cell survival under oxidative stress. The peptide did not directly stimulate fibroblast proliferation, suggesting that its effects were mediated through improved cell viability and migration rather than increased cell division. The study also identified activation of the focal adhesion kinase (FAK)-paxillin signalling pathway, providing mechanistic insight into how BPC-157 may influence tendon repair and connective tissue regeneration. [1]
A subsequent study by the same research group demonstrated that BPC-157 increased growth hormone receptor (GHR) expression in tendon fibroblasts at both the mRNA and protein levels. By increasing GHR availability, pretreatment with BPC-157 enhanced growth hormone-induced activation of the downstream JAK2 signalling pathway, providing additional mechanistic evidence for the peptide's role in tendon biology and connective tissue research. [2]
A recent narrative review evaluated the expanding body of preclinical research investigating BPC-157 across tendon, ligament, muscle, bone, and cartilage models. The authors concluded that the available experimental evidence demonstrates considerable regenerative potential across multiple musculoskeletal tissues while emphasising that the literature remains predominantly preclinical and that well-designed human clinical trials are still required before clinical conclusions can be drawn. The review highlights BPC-157 as an important research tool for investigating regenerative biology and connective tissue physiology rather than an established therapeutic agent. [3]
TB-500 is a synthetic peptide corresponding to the biologically active region of thymosin beta-4 (Tβ4), a naturally occurring peptide involved in actin regulation, cell migration, and tissue remodelling. Consequently, much of the scientific understanding of TB-500 is derived from the extensive body of research investigating thymosin beta-4 rather than TB-500 itself.
These studies have established the biological rationale for investigating TB-500 in regenerative biology, wound repair, and connective tissue research.
One of the earliest landmark studies demonstrated that thymosin beta-4 accelerated wound healing in a rat full-thickness wound model. Treatment enhanced re-epithelialisation, increased wound contraction, promoted collagen deposition, stimulated angiogenesis, and significantly increased keratinocyte migration. These findings established thymosin beta-4 as an important research model for investigating tissue repair, vascular biology, and regenerative processes. [4]
This comprehensive review evaluated numerous preclinical studies investigating thymosin beta-4 across dermal, corneal, cardiac, and other regenerative models. Collectively, the reviewed evidence demonstrated consistent roles for thymosin beta-4 in cell migration, angiogenesis, cytoskeletal organisation, inflammatory regulation, and tissue remodelling. The review also highlighted the peptide's interaction with G-actin as a fundamental mechanism underlying its biological activity, providing much of the scientific foundation for subsequent research involving TB-500 and related peptide analogues. [5]
The observations discussed in this section are presented solely to summarise the current scientific literature and should not be interpreted as evidence of clinical efficacy or therapeutic use. The BPC-157 & TB-500 blend is supplied exclusively as a laboratory research reagent and is not authorised for human or veterinary use.
The BPC-157 & TB-500 blend is used in laboratory research to investigate multiple aspects of regenerative biology and tissue repair. Because the constituent peptides have distinct but complementary biological properties, researchers frequently study them together to explore how different cellular pathways contribute to healing, tissue remodelling, and structural recovery.
These research applications are based primarily on preclinical studies of the individual peptides rather than dedicated investigations of the combination. They are presented solely to describe the current scientific literature and should not be interpreted as implying clinical efficacy, therapeutic benefit, or authorised medical use.
BPC-157 and TB-500 are widely investigated in experimental models of tendon and ligament repair. Research has examined their influence on fibroblast activity, collagen organisation, extracellular matrix remodelling, and the restoration of connective tissue structure following injury. Studying the peptides together enables researchers to investigate multiple biological processes involved in musculoskeletal regeneration within a single experimental framework.
Experimental studies have explored the role of both peptides in skeletal muscle repair, tissue remodelling, and recovery following acute injury. BPC-157 research has focused primarily on growth factor signalling and tissue integrity, while TB-500 has been investigated for its role in cytoskeletal organisation and cellular migration. Together, these complementary areas of research contribute to a broader understanding of regenerative responses in muscle tissue.
Formation of new blood vessels is an essential component of tissue repair. BPC-157 has been investigated for its interactions with angiogenic signalling pathways and endothelial function, whereas research involving thymosin beta-4, which is the parent peptide from which TB-500 is derived, has demonstrated important roles in endothelial cell migration and vascular remodelling. These complementary research areas make the blend valuable for investigating vascular adaptation during regenerative processes.
One of the distinguishing characteristics of TB-500 research is its relationship with actin dynamics and cellular movement. In contrast, BPC-157 has been studied for its influence on cellular survival, tissue organisation, and connective tissue homeostasis. Investigating these peptides together allows researchers to examine how coordinated cell migration and structural remodelling contribute to tissue regeneration.
The primary scientific rationale for combining BPC-157 and TB-500 is that both peptides influence different aspects of regenerative physiology. By incorporating both peptides into a single research formulation, investigators can study complementary signalling pathways involved in connective tissue biology, vascular adaptation, extracellular matrix organisation, and cellular repair while maintaining consistent experimental conditions.
The BPC-157 & TB-500 blend combines two peptides that influence different aspects of tissue biology through distinct molecular pathways. Although both are widely investigated in regenerative research, they are structurally unrelated and do not share a common mechanism of action.
The scientific rationale for combining BPC-157 and TB-500 in this blend lies in their complementary roles in connective tissue physiology, cellular migration, angiogenesis, and tissue remodelling.
BPC-157 is believed to influence multiple signalling pathways involved in tissue repair. Experimental research has investigated its interactions with nitric oxide signalling, vascular endothelial growth factor (VEGF), focal adhesion kinase (FAK)-paxillin signalling, and growth hormone receptor (GHR)-related pathways. These mechanisms have been associated with angiogenesis, fibroblast migration, collagen organisation, and connective tissue homeostasis in preclinical models. Although the peptide's precise molecular target has not yet been identified, the available evidence suggests that BPC-157 acts through coordinated modulation of several biological pathways involved in tissue repair. [6]
TB-500 is a synthetic peptide derived from the biologically active region of thymosin beta-4. Much of its proposed mechanism is inferred from the extensive literature on thymosin beta-4, which binds and sequesters globular actin (G-actin), helping regulate actin polymerisation, cytoskeletal organisation, and cellular migration. These processes are fundamental to tissue development, wound repair, angiogenesis, and the coordinated movement of cells during regenerative responses. [7]
Experimental research has also associated thymosin beta-4 with modulation of inflammatory signalling, endothelial cell migration, extracellular matrix remodelling, and the activation of pathways involved in tissue regeneration. Consequently, studies investigating TB-500 have focused on its potential role in cellular movement, tissue remodelling, angiogenesis, and wound healing, although the precise molecular mechanisms of the synthetic peptide remain incompletely characterised. [8]
In short, BPC-157 research is mostly centred on growth factor signalling, nitric oxide pathways, and connective tissue physiology, while TB-500 is primarily associated with the structural processes that enable cells to migrate, reorganise their cytoskeleton, and coordinate tissue remodelling during regeneration.
The scientific rationale for combining BPC-157 and TB-500 is based on complementary biology rather than overlapping mechanisms. Studying both peptides within the same experimental system enables researchers to investigate how these distinct biological processes interact during tissue repair and regenerative responses.
This complementary approach has contributed to the blend's popularity in laboratory research, where investigators seek to examine multiple components of tissue regeneration within a single experimental framework.
BPC-157 and TB-500 are frequently investigated together because they influence different aspects of regenerative biology. While BPC-157 research has focused primarily on connective tissue physiology and cellular signalling, TB-500 research has centred on cytoskeletal organisation and cellular migration. The comparison below highlights how the blend differs from its constituent peptides and another widely studied regenerative research peptide.
BPC-157 & TB-500 Blend | ||||
|---|---|---|---|---|
Peptide class | Synthetic gastric pentadecapeptide | Synthetic peptide corresponding to the biologically active region of thymosin beta-4 | Naturally occurring copper-binding tripeptide | Dual-peptide research formulation |
Origin | Derived from a naturally occurring gastric protein fragment | Derived from the biologically active region of thymosin beta-4 | Naturally occurring human copper peptide | Combination of BPC-157 and TB-500 in equal proportions |
Peptide length | 15 amino acids | 43 amino acids | 3 amino acids | 15- and 43-amino-acid peptides |
Primary biological focus | Connective tissue biology, angiogenesis, nitric oxide signalling | Cell migration, cytoskeletal organisation, tissue remodelling | Tissue remodelling, extracellular matrix biology, collagen synthesis | Investigation of complementary regenerative pathways |
Primary mechanism | Multiple signalling pathways under investigation | Mechanism inferred largely from thymosin beta-4 biology; associated with G-actin regulation and cellular migration | Modulation of gene expression, copper transport, and extracellular matrix remodelling | Combines the independent biological properties of both constituent peptides |
Primary research applications | Tendon, ligament, muscle, gastrointestinal and vascular biology | Tissue remodelling, wound repair, angiogenesis, and regenerative biology | Skin biology, connective tissue research, wound healing, and regenerative biology | Integrated models of connective tissue repair and regenerative biology |
Although the names are often used interchangeably within the research community, TB-500 and thymosin beta-4 are not the same compound. Thymosin beta-4 (Tβ4) is a naturally occurring 43-amino-acid peptide expressed in many mammalian tissues and is responsible for much of the published literature describing actin regulation, cell migration, angiogenesis, and tissue repair. On the other hand, TB-500 is a synthetic peptide developed from the biologically active region of thymosin beta-4 and is intended to reproduce many of the biological properties associated with the parent peptide in experimental research.
This distinction is important when interpreting published studies. Much of the mechanistic understanding commonly attributed to TB-500 is derived from investigations of thymosin beta-4 rather than direct studies of the synthetic peptide itself. Consequently, references to TB-500 frequently rely on the broader body of thymosin beta-4 research to explain its proposed biological activity and scientific rationale.
Crystal Peptides is committed to providing research peptides that meet high standards of analytical quality, consistency, and traceability. Every batch of this BPC-157 & TB-500 5/5mg blend undergoes HPLC purity analysis and independent third-party verification by accredited laboratories, including Janoshik Analytical.
Testing may include peptide identity, peptide content, sterility, endotoxin, and heavy metal screening, with Certificates of Analysis provided for every batch to help researchers verify the analytical characteristics of the exact material supplied.
Because this formulation contains two independently characterised peptides, analytical testing should verify both the identity and quality of each constituent peptide. Researchers should look for analytical data including:
Reviewing these analytical results together provides substantially greater confidence than relying on a reported purity percentage alone, helping researchers confirm the identity, composition, and overall analytical quality of the material before incorporating it into experimental work.
For proper handling and storage, the BPC-157 & TB-500 blend is supplied as a co-lyophilised powder and should be stored sealed, dry, protected from light, and preferably at -20°C or below until required for research.
Reconstitute with bacteriostatic water or sterile water, after which the solution should be refrigerated at 2–8°C, handled using appropriate laboratory techniques, and used according to the laboratory's established stability protocols. Avoid repeated freeze-thaw cycles, prolonged exposure to elevated temperatures, and vigorous agitation as these practices may contribute to peptide degradation and reduce long-term stability.
All products supplied by Crystal Peptides are intended exclusively for research and development purposes. They are provided solely as laboratory research reagents for use by qualified professionals in controlled scientific settings and are not supplied for human or veterinary use.
This product is not a medicinal product, food, food supplement, medical device, cosmetic, or veterinary medicine. The information presented on this page is provided exclusively to summarise the current scientific literature and should not be interpreted as evidence of clinical efficacy, therapeutic benefit, or authorised medical use. Any references to published studies describe experimental research only and have not been evaluated by the European Medicines Agency (EMA) or any other medicines regulator for clinical application.
The BPC-157 & TB-500 blend has not been evaluated as a combined formulation in clinical studies and has not been authorised as a medicinal product by the European Medicines Agency (EMA), the U.S. Food and Drug Administration (FDA), or any other major medicines regulator. The scientific rationale for this formulation is derived primarily from published preclinical investigations of the individual constituent peptides rather than dedicated studies of the combination itself. Crystal Peptides supplies this blend exclusively for laboratory research and development.
Researchers and purchasers are responsible for ensuring that the acquisition, importation, storage, handling, use, and disposal of research materials comply with all applicable national and local laws and regulations. Because legislation governing research chemicals differs between jurisdictions, customers should confirm the legal requirements applicable within their own country before purchasing or importing laboratory reagents.
The BPC-157 & TB-500 blend is a dual-peptide research formulation that combines equal amounts of BPC-157 and TB-500 within a single co-lyophilised vial. The formulation is available in 5/5 mg and 10/10 mg strengths and allows researchers to investigate two complementary peptide classes within the same experimental model. While BPC-157 has been studied primarily in connective tissue biology, angiogenesis, and growth factor signalling, TB-500 research has focused on cytoskeletal organisation, cell migration, and tissue remodelling. The blend is supplied exclusively for laboratory research and is not authorised for human or veterinary use.
Yes. Wolverine Blend is a commercial nickname commonly used within the research peptide market to describe formulations containing both BPC-157 and TB-500. It is not a separate peptide or a distinct molecular entity, nor does it refer to a standardised formulation recognised by scientific or regulatory organisations. Regardless of the name used, researchers should verify the composition, peptide ratio, analytical testing, and Certificate of Analysis supplied with each product before use in laboratory research.
Although the terms are often used interchangeably, TB-500 and thymosin beta-4 (Tβ4) are not identical. Thymosin beta-4 is a naturally occurring 43-amino-acid peptide expressed in many mammalian tissues and is responsible for much of the published literature describing actin regulation, angiogenesis, cell migration, and tissue repair. TB-500 is a synthetic peptide developed from the biologically active region of thymosin beta-4 and is intended to reproduce many of the biological properties associated with the parent peptide. Consequently, much of the mechanistic understanding of TB-500 is derived from studies of thymosin beta-4 rather than direct investigations of the synthetic peptide itself.
At present, there are no published clinical trials specifically evaluating the BPC-157 & TB-500 blend as a combined formulation. The scientific rationale for the blend is derived primarily from preclinical investigations of the individual constituent peptides, which have been studied separately in models of connective tissue biology, angiogenesis, cell migration, and regenerative processes. Consequently, the available evidence should not be interpreted as demonstrating clinical efficacy or therapeutic benefit for the combination.
Yes. Every batch is accompanied by a batch-specific Certificate of Analysis (COA) that can be traced directly to the independent testing laboratory. The COA enables researchers to verify the identity, purity, and analytical characteristics of the exact batch supplied before incorporating it into experimental work. Crystal Peptides also maintains a dedicated Lab Tests page, allowing researchers to review analytical documentation and confirm batch-specific testing results.
Each batch of BPC-157 & TB-500 combo for sale by Crystal Peptides undergoes comprehensive analytical testing before release. Quality control includes HPLC purity analysis to assess chromatographic purity and LC-MS to verify the molecular identity of both BPC-157 and TB-500. Depending on the batch, additional testing may include peptide content, sterility, endotoxin, and heavy metal screening. Independent third-party verification by accredited laboratories such as Janoshik Analytical provides researchers with confidence in the identity, purity, and overall analytical quality of the material supplied.
Crystal Peptides currently supplies the BPC-157 & TB-500 blend in 5/5 mg and 10/10 mg co-lyophilised research vials, with each formulation containing equal amounts of both constituent peptides. Current availability, pricing, and batch-specific analytical documentation are provided on the product page, allowing researchers to select the formulation most appropriate for their experimental requirements.
The BPC-157 & TB-500 blend is supplied as a co-lyophilised powder and is typically reconstituted in laboratory settings using bacteriostatic water or sterile water. The diluent should be introduced slowly down the inside wall of the vial to minimise foaming, after which the peptide should be allowed to dissolve naturally without vigorous agitation. Following reconstitution, the solution should be refrigerated at 2–8°C and handled using appropriate laboratory procedures. Unreconstituted vials should be stored sealed, dry, protected from light, and preferably at -20°C or below. Repeated freeze-thaw cycles and prolonged exposure to elevated temperatures should be avoided to help preserve peptide integrity.
Researchers throughout the European Union can buy BPC-157 & TB-500 blend from Crystal Peptides as a high-purity research formulation supplied exclusively for laboratory research. The company is committed to analytical transparency, traceable quality documentation, and reliable fulfilment, making it a trusted source of research peptides for universities, laboratories, and independent researchers across Europe.
Yes. Crystal Peptides ships the BPC-157 & TB-500 blend throughout Europe using discreet packaging and tracked delivery services. Orders are typically dispatched promptly, with delivery times varying by destination country, and express shipping is available for many European locations. Researchers can review shipping options, estimated delivery times, accepted payment methods, and country-specific ordering information before placing an order.
For analytical, biochemical or non-clinical laboratory research only. Not for human or veterinary use. Not for ingestion, injection, topical application, inhalation, diagnostic, therapeutic, prophylactic or cosmetic use.