BPC-157 + TB-500

BPC-157 + TB-500 is supplied as a laboratory research reference material for in-vitro and laboratory research use only. This two-peptide kit pairs BPC-157, a 15-residue synthetic peptide with the sequence GEPPPGKPADDAGLV, molecular formula C62H98N16O22 and molecular weight of approximately 1419 g/mol (CAS 137525-51-0), with TB-500, a 43-residue N-acetylated peptide bearing the sequence Ac-SDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES, molecular formula C212H350N56O78S and molecular weight of approximately 4963 g/mol (CAS 77591-33-4). Both items are provided as white to off-white lyophilized powders of synthetic origin, produced by solid-phase peptide synthesis and purified to not less than 98% by reversed-phase HPLC, with lot-specific identity and purity data documented on the Certificate of Analysis.

Structurally, the BPC-157 + TB-500 pairing places two very different peptide scaffolds side by side for comparative analytical work. BPC-157 is a short, proline-rich sequence with three consecutive prolines flanking a central lysine and an acidic ADDA motif, features that contribute to a compact conformation, relatively high aqueous solubility and a characteristic reversed-phase HPLC retention profile. TB-500 is a considerably larger, highly charged polypeptide dominated by lysine, glutamate and aspartate residues, with an N-terminal acetyl cap and a single methionine that is often monitored as an oxidation-prone site during stability and forced-degradation studies. The disparity in mass, isoelectric behavior and hydrophobicity between the two peptides makes this complex a useful reference set for method development across chromatography, mass spectrometry and UV spectrophotometry workflows.

Analytically, BPC-157 + TB-500 supports identity confirmation by high-resolution ESI-MS (with monoisotopic and average mass windows appropriate to each component), sequence verification by MS/MS or Edman chemistry, and purity assessment by orthogonal RP-HPLC gradients. Residual solvent, water content by Karl Fischer, counter-ion content (typically trifluoroacetate or acetate depending on the lot) and peptide net content by nitrogen or amino acid analysis can all be evaluated against the values reported on the Certificate of Analysis. The lyophilized physical form supports gravimetric handling in a controlled laboratory environment, and both peptides are typically reconstituted in bacteriostatic-free aqueous or dilute acetic acid buffers for analytical characterization; stock solutions should be prepared, aliquoted and stored under conditions consistent with the user's validated laboratory procedures.

Published scientific literature has examined BPC-157 + TB-500 in preclinical research contexts, and this reference material is offered to support in-vitro assay development, reference-standard qualification, chromatographic method validation, stability screening and other bench-scale characterization studies. PEPTIDE.Power makes no therapeutic, diagnostic, or efficacy claims regarding BPC-157 + TB-500 and provides no administration or dosing guidance. This material is not a drug, supplement, cosmetic, or food, and is not intended for human or veterinary use, injection, or ingestion. Full identity and purity documentation is available on the lot-specific Certificate of Analysis on request.

Supplied as a lyophilized (freeze-dried) powder in a sealed vial. A research reference material - not a finished product and not a delivery device. Net contents per unit are shown in the product options.

Store the sealed lyophilized powder at -20 C, protected from light and moisture. After reconstitution for laboratory use, keep cold and use promptly. Handle per standard laboratory practice; a Safety Data Sheet (SDS) is available on request.

This material is sold to qualified laboratory and research buyers for lawful research use only. It is not a drug, supplement, cosmetic, or food, and is not for human or veterinary use, injection, or ingestion. By purchasing, you confirm you are 21 or older and will use this material only for lawful laboratory research.