Wolverine Blend (BPC-157 + TB-500) Molecular Weight, Sequence & CAS Reference

1. Characterization of the Dual-Peptide Research Matrix

The designation 'Wolverine Blend' refers to a co-lyophilized research matrix combining two distinct synthetic signaling peptides: BPC-157 (Body Protection Compound 157) and TB-500 (synthetic Thymosin Beta-4). Rather than existing as a singular hybridized chemical entity or covalently conjugated molecule, this reagent is a physical mixture prepared in precise stoichiometric mass ratios within laboratory settings—typically 5 mg of BPC-157 combined with 5 mg of TB-500.

Because the compound consists of two independent polypeptide chains co-formulated in a single vial, analytical characterization requires evaluating each individual peptide constituent independently. Laboratory investigators evaluating our product/bpc-157-5mg-tb-500-5mg-wolverine-blend must utilize analytical methods capable of resolving both targets simultaneously, such as reverse-phase high-performance liquid chromatography (RP-HPLC) paired with electrospray ionization mass spectrometry (ESI-MS).

2. Primary Amino Acid Sequences and Structural Topologies

The first active component of the matrix, BPC-157, is a 15-amino acid fragment derived from human gastric juice protein BPC. Its primary linear sequence is represented as: Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val (single-letter code: GEPPPGKPADDAGLV). The molecular structure lacks disulfide bridges, but exhibits stable secondary conformations in aqueous solutions due to the concentration of proline residues in its N-terminal region.

The second component, TB-500, corresponds to the full-length synthetic sequence of Thymosin Beta-4, an acetylated 44-amino acid polypeptide. Its linear primary sequence is: 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 (single-letter code: Ac-SDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES). In some literature contexts, short actin-binding motifs such as LKKTETQ are investigated; however, standard synthetic TB-500 research reagents represent the complete 44-residue structure. For broader structural catalogs, consult our full all-peptides directory.

3. Molecular Weight and Empirical Formula Specifications

Because the combination matrix contains two separate molecular structures, there is no single unified molecular formula or molecular weight for the mixture as a whole. Instead, each constituent maintains its specific physical constants:

BPC-157 Monoisotopic/Average Mass: Empirical Formula: C62H98N16O22. The exact monoisotopic mass is 1418.70 g/mol, with a calculated average molecular weight of approximately 1419.53 g/mol.

TB-500 (Thymosin Beta-4) Monoisotopic/Average Mass: Empirical Formula: C212H350N56O78S. The exact monoisotopic mass is 4960.50 g/mol, with a calculated average molecular weight of approximately 4963.50 g/mol.

When performing quantitative assays or stoichiometry calculations for research-peptides/bpc-157 or research-peptides/tb-500 within the combined matrix, scientists must calculate molar concentrations independently based on these distinct molecular masses rather than attempting to average the total gross mass of the vial.

4. CAS Registry Numbers and Nomenclature Systems

A standard common misconception in chemical cataloging is expecting a single Chemical Abstracts Service (CAS) registry number for a non-covalent multi-component blend. The Wolverine Blend itself does not possess a single assigned CAS registry number because it is an ad-hoc laboratory formulation. Chemical identification relies on the individual CAS numbersassigned to each component:

BPC-157 Free Base / Acetate CAS Number: 137525-51-0. Alternative chemical identifiers include PL 14736, PL-10, and Bepecin.

TB-500 / Thymosin Beta-4 CAS Number: 77591-33-4. Alternative chemical identifiers include Thymosin β4 synthetic, FX peptide, and TMSB4X.

In analytical reporting and institutional safety protocols, both CAS registry numbers should be recorded to ensure proper regulatory and chemical inventory compliance for laboratory environments.

5. Salt Form Variations and Net Peptide Content

Synthetic peptides manufactured via solid-phase peptide synthesis (SPPS) undergo cleavage and purification processes that introduce counter-ions to stabilize basic amino acid residues (such as Lysine and Arginine). The raw lyophilized cake contains net peptide active content along with counter-ions and trace bound moisture.

Trifluoroacetate (TFA) Salt vs. Acetate Salt: The primary salt form resulting from standard RP-HPLC purification using trifluoroacetic acid is the TFA salt form. For sensitive cell culture models, peptides are frequently converted to an acetate salt form via ion-exchange chromatography. TFA counter-ions generally represent 10% to 25% of the total mass of the lyophilized powder.

Calculating Net Peptide Content: If a vial contains 10 mg of gross co-lyophilized material (5 mg BPC-157 + 5 mg TB-500) with an average net peptide purity factor of 82% (18% salt counter-ions and residual hydration), the true combined net peptide mass is approximately 8.2 mg. Researchers conducting quantitative assay experiments must verify the exact net peptide factor using the batch-specific Certificate of Analysis available on our coa page.

6. Analytical Spectrometry and HPLC Characterization

Analytical validation of a dual-peptide blend requires chromatographical separation prior to mass determination. Standard laboratory analytical protocols utilize C18 reverse-phase HPLC columns with a linear gradient of acetonitrile (0.1% TFA) in water (0.1% TFA).

Chromatographic Resolution: Under standardized C18 reverse-phase conditions, BPC-157 (1419.53 g/mol) elutes earlier due to its moderate hydrophobicity profile, whereas the larger 44-amino acid TB-500 (4963.50 g/mol) exhibits a distinct, separate retention time. Single-peak observations indicate either incomplete separation or improper column chemistry.

Mass Spectrometry (ESI-MS): Electrospray ionization mass spectrometry of the mixture reveals multi-charged species. BPC-157 typically demonstrates prominent [M+H]+ (m/z ~1420.5) and [M+2H]2+ (m/z ~710.8) ions. TB-500 displays higher-charge states, including [M+4H]4+ (m/z ~1241.9), [M+5H]5+ (m/z ~993.7), and [M+6H]6+ (m/z ~828.3). Spectroscopic data must match these exact mass charge ratios to confirm structural identity.

7. Reconstitution Mathematics and Solution Mechanics

Reconstitution of a multi-peptide lyophilized matrix requires precise fluid volume handling to achieve predictable target concentrations for in vitro assays. Because both peptides are co-lyophilized in equal mass amounts (e.g., 5 mg BPC-157 and 5 mg TB-500, totaling 10 mg active peptide), adding a specific volume of bacteriostatic or sterile laboratory water affects the concentration of both components equally in terms of mass-per-volume, though not in molarity.

For instance, reconstituting a 5mg/5mg blend with 2.0 mL of sterile diluent yields a final mass concentration of 2.5 mg/mL for BPC-157 and 2.5 mg/mL for TB-500. Due to the disparity in molecular weight (1419.53 g/mol vs 4963.50 g/mol), the resulting molarity of BPC-157 will be approximately 3.5 times higher than that of TB-500 in the same solution volume. To calculate precise diluent volumes and molar conversions for laboratory research protocols, utilize our interactive reconstitution-calculator.

8. Structural Comparisons to Related Regenerative Research Peptides

When evaluating tissue-repair mechanisms and cytoprotective signaling pathways in preclinical models, researchers frequently compare the BPC-157/TB-500 matrix with other signaling peptides. Key compounds in this analytical space include research-peptides/ghrp-6, growth hormone secretagogues, and copper-binding peptides like GHK-Cu.

Unlike small hexapeptides like GHRP-6 (MW 873.01 g/mol) that act primarily via ghrelin receptor (GHS-R1a) binding, or tripeptide complexes like GHK-Cu (MW 403.93 g/mol) that rely on divalent metal chelation, the Wolverine Blend matrix combines focal adhesion modulation (BPC-157) with G-actin sequestration and cell migration signaling (TB-500). Detailed biochemical pathways can be explored further in our open-access research library.

9. Lyophilized Stability Metrics and Storage Parameters

Lyophilized peptide mixtures are susceptible to temperature, light, and moisture-induced degradation paths, including deamidation (at Asp/Asn residues) and oxidation (specifically at the Methionine residue at position 6 of TB-500).

Desiccated Storage: Lyophilized cakes should be stored at -20°C for short-to-medium term storage, or -80°C for long-term preservation. Under desiccated sub-zero conditions, chemical stability is maintained for up to 24 months.

Reconstituted Solution Stability: Once reconstituted in sterile or bacteriostatic diluent, solutions should be kept at 2°C to 8°C and used within 28 days. Repeated freeze-thaw cycles cause physical shearing and aggregation of the 44-amino acid TB-500 chain and should be strictly avoided in analytical protocols.

10. Quality Control Protocols and PX1 Research Standards

PX1 Research enforces strict analytical standards for all research compounds supplied to academic, institutional, and private laboratory facilities. Every production batch of Wolverine Blend undergoes independent testing in an ISO 17025 accredited laboratory facility.

Verification Standards: Raw purity is verified to exceed 99.0% using RP-HPLC with photodiode array detection. Molecular mass is confirmed via ESI-MS, and bacterial endotoxin levels are verified to remain strictly below industry thresholds (<0.05 EU/mg) using chromogenic LAL assays. Bulk inquiries and institutional purchasing details can be reviewed at our wholesale portal.