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BPC-157 10MG + TB-500 10MG - Wholesale
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$75.00
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$150.00
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BPC-157 10MG + TB-500 10MG - Wholesale
Overview
The BPC-157/TB-500 combination, sometimes referred to as the Wolverine Blend, pairs two distinct synthetic peptides studied for their complementary roles in tissue repair, angiogenesis, and recovery. BPC-157 is a synthetic 15-amino acid pentadecapeptide derived from a protein fragment found in human gastric juice. TB-500 is a synthetic analog of thymosin beta-4 (Tβ4), a naturally occurring actin-binding protein involved in cellular migration and tissue organization. Neither peptide is FDA-approved for human use; BPC-157 was classified as a Category 2 bulk drug substance by the FDA in 2023.
Mechanism of Action
BPC-157 promotes local tissue healing by upregulating growth hormone receptors in fibroblasts, stimulating collagen synthesis, modulating angiogenesis via nitric oxide and VEGF pathways, and exerting anti-inflammatory effects on oxidative and cytokine signaling cascades. It also supports gastrointestinal mucosal integrity.
TB-500 operates systemically by promoting actin cytoskeletal reorganization, cell migration, and new blood vessel formation. As a thymosin beta-4 analog, it supports extracellular matrix remodeling, reduces fibrotic scarring, and enhances tissue elasticity and functional recovery.
When used in combination, BPC-157 tends to exert more localized effects at the injury site while TB-500 supports systemic recovery across multiple tissue types, creating a complementary healing response.
Research and Off-Label Applications
Musculoskeletal injury repair (tendon, ligament, muscle), post-surgical recovery, chronic joint pain and inflammation, gut and mucosal healing (BPC-157), cardiovascular protection and cardiac recovery (TB-500), and anti-aging tissue regeneration.
Administration
Administered as two separate subcutaneous injections. Protocols commonly utilize 10 mg of each compound. Peak results are typically observed 4–8 weeks into therapy. Clinical protocols generally recommend limiting continuous use to 90 days followed by a 30-day washout period.
Potential Adverse Effects
Generally well tolerated in available research. Potential concerns include theoretical promotion of angiogenesis in the context of undetected malignancy, mild injection site reactions, and fatigue. The combination should not be used in individuals with active cancer without specialist guidance. Long-term human safety data is limited.
Properties
1. Basic Information
2. Structural Properties BPC-157 Peptide Nature: Linear 15-amino acid peptide; no disulfide bonds; proline-rich sequence (three consecutive prolines at positions 3–5) confers conformational rigidity in the central region; derived from the amino acid sequence of a protein found in human gastric juice (BPC protein)
TB-500 Peptide Nature: Linear 43-amino acid peptide; N-terminally acetylated; sequence corresponds to residues 17–23 of thymosin beta-4 (the actin-binding domain) extended to include flanking regions; no disulfide bonds; rich in acidic and basic residues contributing to a highly charged surface profile
Secondary Structure: BPC-157: largely unstructured in free solution; proline clusters restrict backbone flexibility in the central domain. TB-500: adopts a predominantly α-helical conformation in the actin-binding region; helical structure is proposed to mediate G-actin sequestration in experimental models
Hydrophobicity: BPC-157: moderately hydrophilic; leucine and valine at C-terminus introduce minor hydrophobic character. TB-500: amphipathic; hydrophobic face of the central helix is proposed to mediate actin binding while the hydrophilic face supports aqueous solubility
Charge: BPC-157: net negative charge at physiological pH due to glutamate and aspartate residues. TB-500: net positive to neutral charge at physiological pH; multiple lysine residues (Lys3, Lys6, Lys9, Lys10, Lys14, Lys16) dominate the charge profile
3. Solubility
4. Stability BPC-157 Thermal Stability: Sensitive to elevated temperatures; refrigerate after reconstitution; proline-rich sequence contributes to resistance against certain proteolytic enzymes but does not confer general thermal stability
BPC-157 Proteolytic Stability: Proline clusters at positions 3–5 confer resistance to prolyl endopeptidase cleavage within this region; overall proteolytic stability moderate; gastric acid stability reported in animal model studies, consistent with the peptide's origin from a gastric protein
TB-500 Thermal Stability: Moderately stable in aqueous solution at refrigerated temperatures; sensitive to elevated temperatures and prolonged storage at room temperature
TB-500 Proteolytic Stability: Susceptible to endopeptidase activity in biological matrices; N-terminal acetylation provides protection against aminopeptidase degradation; plasma half-life not definitively characterized in published literature
Storage: Store both components lyophilized at −20°C protected from light; reconstituted BPC-157 stable up to 14 days at 2–8°C; reconstituted TB-500 stable up to 7–14 days at 2–8°C; avoid repeated freeze-thaw cycles for both components
5. Chemical Reactivity BPC-157 contains no cysteine or methionine residues; oxidative degradation risk is low; no disulfide bonds to reduce or oxidize
TB-500 contains methionine (Met-6); susceptible to oxidation to methionine sulfoxide under peroxide-containing or strongly aerobic conditions; protect from oxidative environments
BPC-157 aspartate and glutamate residues may undergo deamidation under acidic or elevated temperature conditions; maintain neutral pH and refrigerated storage
Both peptides are stable under physiological pH conditions; hydrolysis risk increases under strongly acidic or alkaline conditions
No reactive cross-linking groups in either peptide; the combination does not form covalent intermolecular bonds under standard research handling conditions
6. Other Properties
- Name: BPC-157 + TB-500 Combination (Wolverine Blend); BPC-157: Body Protection Compound-157; TB-500: Thymosin Beta-4 synthetic analog
- Type: Dual synthetic research peptide combination; tissue repair and regeneration research material
- Length: BPC-157: 15 amino acids; TB-500: 43 amino acids
- Sequence: BPC-157: Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val; TB-500: 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 Weight: BPC-157: ~1,419 Da; TB-500: ~4,963 Da
- Formula: BPC-157: C₆₂H₉₈N₁₆O₂₂; TB-500: C₂₁₂H₃₅₀N₅₆O₇₈S
2. Structural Properties BPC-157 Peptide Nature: Linear 15-amino acid peptide; no disulfide bonds; proline-rich sequence (three consecutive prolines at positions 3–5) confers conformational rigidity in the central region; derived from the amino acid sequence of a protein found in human gastric juice (BPC protein)
TB-500 Peptide Nature: Linear 43-amino acid peptide; N-terminally acetylated; sequence corresponds to residues 17–23 of thymosin beta-4 (the actin-binding domain) extended to include flanking regions; no disulfide bonds; rich in acidic and basic residues contributing to a highly charged surface profile
Secondary Structure: BPC-157: largely unstructured in free solution; proline clusters restrict backbone flexibility in the central domain. TB-500: adopts a predominantly α-helical conformation in the actin-binding region; helical structure is proposed to mediate G-actin sequestration in experimental models
Hydrophobicity: BPC-157: moderately hydrophilic; leucine and valine at C-terminus introduce minor hydrophobic character. TB-500: amphipathic; hydrophobic face of the central helix is proposed to mediate actin binding while the hydrophilic face supports aqueous solubility
Charge: BPC-157: net negative charge at physiological pH due to glutamate and aspartate residues. TB-500: net positive to neutral charge at physiological pH; multiple lysine residues (Lys3, Lys6, Lys9, Lys10, Lys14, Lys16) dominate the charge profile
3. Solubility
- BPC-157: Soluble in sterile water and physiological saline; optimal solubility at pH 5.5–7.5; recommended reconstitution in bacteriostatic water at 1–5 mg/mL
- TB-500: Highly soluble in sterile water and aqueous buffers due to highly charged surface; solubility exceeds 5 mg/mL under standard conditions; reconstitution in sterile water recommended
- Both components supplied as lyophilized white to off-white powders; reconstituted separately prior to research use
4. Stability BPC-157 Thermal Stability: Sensitive to elevated temperatures; refrigerate after reconstitution; proline-rich sequence contributes to resistance against certain proteolytic enzymes but does not confer general thermal stability
BPC-157 Proteolytic Stability: Proline clusters at positions 3–5 confer resistance to prolyl endopeptidase cleavage within this region; overall proteolytic stability moderate; gastric acid stability reported in animal model studies, consistent with the peptide's origin from a gastric protein
TB-500 Thermal Stability: Moderately stable in aqueous solution at refrigerated temperatures; sensitive to elevated temperatures and prolonged storage at room temperature
TB-500 Proteolytic Stability: Susceptible to endopeptidase activity in biological matrices; N-terminal acetylation provides protection against aminopeptidase degradation; plasma half-life not definitively characterized in published literature
Storage: Store both components lyophilized at −20°C protected from light; reconstituted BPC-157 stable up to 14 days at 2–8°C; reconstituted TB-500 stable up to 7–14 days at 2–8°C; avoid repeated freeze-thaw cycles for both components
5. Chemical Reactivity BPC-157 contains no cysteine or methionine residues; oxidative degradation risk is low; no disulfide bonds to reduce or oxidize
TB-500 contains methionine (Met-6); susceptible to oxidation to methionine sulfoxide under peroxide-containing or strongly aerobic conditions; protect from oxidative environments
BPC-157 aspartate and glutamate residues may undergo deamidation under acidic or elevated temperature conditions; maintain neutral pH and refrigerated storage
Both peptides are stable under physiological pH conditions; hydrolysis risk increases under strongly acidic or alkaline conditions
No reactive cross-linking groups in either peptide; the combination does not form covalent intermolecular bonds under standard research handling conditions
6. Other Properties
- Mechanistic complementarity: BPC-157 is described in preclinical literature as primarily exerting localized tissue repair signaling activity (GH receptor upregulation, collagen synthesis, NO/VEGF angiogenesis), while TB-500 is described as operating through systemic actin sequestration, cell migration facilitation, and extracellular matrix remodeling; the combination is investigated in the context of multi-pathway tissue repair research
- BPC-157 regulatory status: Classified as a Category 2 bulk drug substance by the FDA in 2023, prohibiting its use in compounded preparations for human use in the United States; classified as a research-only peptide
- TB-500 relationship to thymosin beta-4: TB-500 is a synthetic research analog of the 17–23 actin-binding domain of thymosin beta-4 (Tβ4); native Tβ4 is a 43-amino acid protein involved in actin dynamics, wound healing, and cardiac repair in physiological contexts
- Combination rationale: The pairing of a localized (BPC-157) and systemic (TB-500) repair-signaling peptide is discussed in preclinical tissue repair literature as a strategy for investigating multi-mechanism recovery pathway interactions
Description
SLU-PP-322 is a synthetic research compound and has been described in the scientific literature as a pan-agonist of estrogen-related receptors (ERRα, ERRβ, ERRγ), nuclear receptors associated with mitochondrial function, oxidative metabolism, and energy expenditure regulation in metabolically active tissues. Publications referencing SLU-PP-322 discuss it in the context of nuclear receptor pharmacology, exercise-associated gene expression programs, and mitochondrial biogenesis signaling within experimental systems.
Reports involving SLU-PP-322 describe its receptor activation characteristics and associated downstream signaling properties under defined experimental conditions. Observations of ERRα-mediated gene expression patterns, oxidative phosphorylation pathway components, fatty acid oxidation signaling markers, and skeletal muscle fiber type remodeling indicators are limited to non-clinical research settings and are reported as descriptive findings within cellular and animal model studies.
All references to SLU-PP-322 are confined to mechanistic and observational research contexts and do not extend beyond laboratory-based investigation.
In the scientific literature, SLU-PP-322 has been referenced in non-clinical research involving nuclear receptor binding assays, gene expression profiling studies, and preclinical metabolic and cardiac animal models. These publications describe experimental contexts in which molecular interactions, transcriptional activation markers, and pathway-associated signaling components were observed and recorded.
Reported research contexts include examination of:
- ERRα, ERRβ, and ERRγ receptor activation dynamics and associated gene expression patterns in experimental models
- Mitochondrial biogenesis and oxidative phosphorylation pathway markers observed in skeletal and cardiac muscle research settings
- Fatty acid oxidation signaling components and metabolic flexibility indicators evaluated under experimental conditions
- Skeletal muscle fiber type remodeling markers toward oxidative phenotype assessed in preclinical animal contexts
- Cardioprotective signaling pathway components including ejection fraction-associated markers and fibrosis indicators reported in heart failure models
All reported applications are confined to descriptive investigation within controlled laboratory research environments.
Mechanistic discussions in preclinical publications describe SLU-PP-322 as a small molecule ERR pan-agonist in which preferential activation of ERRα (reported at approximately 4-fold selectivity over ERRγ) is described as initiating an aerobic exercise-associated transcriptional program. This activation pattern is discussed in the context of exercise mimetic pharmacology within the cited literature. These descriptions are limited to molecular and biochemical observations within experimental systems and do not imply functional outcomes beyond the reported research context.
SLU-PP-322 is supplied as a research-grade compound material. Identity and composition have been reported as characterized using analytical techniques commonly applied to small molecule research materials, including chromatographic and mass spectrometric methods. Individual laboratories determine handling, storage, and analytical verification parameters in accordance with internal research protocols.
COA
Storage
All of our products are manufactured using the Lyophilization (Freeze Drying) process, which ensures that our products remain 100% stable for shipping for up to 3-4 months. Once the peptides are reconstituted (mixed with bacteriostatic water), they must be stored in the fridge to maintain stability. After reconstitution, the peptides will remain stable for up to 30 days.
Lyophilization is a unique dehydration process, also known as cryodesiccation, where the peptides are frozen and then subjected to low pressure. This causes the water in the peptide vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure known as lyophilized peptide. The puffy white powder can be stored at room temperature until you're ready to reconstitute it with bacteriostatic water.
Once peptides have been received, it is imperative that they are kept cold and away from light. If the peptides will be used immediately, or in the next several days, weeks or months, short-term refrigeration under 4°C (39°F) is generally acceptable. Lyophilized peptides are usually stable at room temperatures for several weeks or more, so if they will be utilized within weeks or months such storage is typically adequate.
For longer term storage (several months to years) it is more preferable to store peptides in a freezer at -80°C (-112°F). When storing peptides for months or even years, freezing is optimal in order to preserve the peptide's stability.
Lyophilization is a unique dehydration process, also known as cryodesiccation, where the peptides are frozen and then subjected to low pressure. This causes the water in the peptide vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure known as lyophilized peptide. The puffy white powder can be stored at room temperature until you're ready to reconstitute it with bacteriostatic water.
Once peptides have been received, it is imperative that they are kept cold and away from light. If the peptides will be used immediately, or in the next several days, weeks or months, short-term refrigeration under 4°C (39°F) is generally acceptable. Lyophilized peptides are usually stable at room temperatures for several weeks or more, so if they will be utilized within weeks or months such storage is typically adequate.
For longer term storage (several months to years) it is more preferable to store peptides in a freezer at -80°C (-112°F). When storing peptides for months or even years, freezing is optimal in order to preserve the peptide's stability.
