ReferenceFeaturedGHK-Cu
Copper tripeptide complex — HPLC-verified, COA per lot.
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Custom blend
Two-peptide research blend — HPLC-verified, lot-traceable.
Custom blendSize
Price
$60.00
SKU TB500-BPC157-5-5
Complimentary shipping over $200
For research use only. Not for human consumption.
Every lot is third-party assayed by HPLC. A lot-specific COA ships with the product and is mirrored to the buyer account.
Real COAs are published per lot when shipments begin. Sample COA available on request.
Scientific Details
This research blend combines two structurally distinct cytoprotective and tissue-response research peptides — TB-500 (the 17-residue active fragment of thymosin β4) and BPC-157 (the 15-residue stable cytoprotective pentadecapeptide) — supplied together as a single lyophilized reference material for combined tissue-response and cytoprotective signaling research. The peer-reviewed literature catalogs this combination class within paradigms that examine actin-binding-driven cellular migration alongside cytoprotective-peptide signaling in the same experimental session, allowing investigators to dissect the contributions of each peptide to downstream tissue-response dynamics. Each component's molecular identity is characterized individually on the supplier's Certificate of Analysis; component-level details (sequence, molecular weight, CAS, PubChem CID) are documented on the individual reference-standard PDPs linked from the composition panel above. The blend is supplied for laboratory characterization, in-vitro signaling assays, and tissue-response research in cell-culture and animal-model contexts only. For research use only; not for human consumption, medical use, or veterinary application.
The blend's combined molecular profile is the sum of two distinct peptide architectures documented across the published literature. TB-500 is a 17-residue linear peptide derived from the actin-binding region of thymosin β4, whose interaction profile centers on G-actin binding with downstream investigations of Rac1, MMP, and VEGF pathway intersection in tissue-response assays. BPC-157 is a 15-residue linear pentadecapeptide whose interaction profile spans nitric-oxide pathway modulation, growth-factor signaling intersection, and angiogenic-marker response in injury-model studies. The two components engage distinct cellular-signaling pathways documented in the literature as relevant to tissue-response research. Pharmacokinetic descriptors for each component are short systemic plasma residence under standard parenteral paradigms. All activity descriptors here are framed as documented in published research rather than as effects of the supplied product.
Experimental domains documented in the published literature for combined TB-500-and-BPC-157 research paradigms include comparative tissue-response studies parsing actin-binding-driven cellular migration from cytoprotective-peptide signaling, in-vitro fibroblast and endothelial-cell migration assays under combined-component exposure, wound-model investigations in rodent contexts, and structure-activity work probing how the two peptide architectures integrate downstream tissue-response signaling. Investigators use blended research materials of this kind to study the additive-versus-distinct-mechanism question across two non-overlapping cellular-signaling profiles. Use in laboratory research extends to mechanism-elucidation paradigms where the blend serves as a defined dual-component tissue-response research reference. The blend is supplied for these and equivalent in-vitro and animal-model experimental contexts only, with no associated guidance for human, clinical, or veterinary application. Researchers should consult component-level PDPs and primary literature when designing context-specific protocols.
Each component of the blend is characterized individually before combination. Reverse-phase HPLC is performed on the lyophilized blend to verify the relative composition ratio of the two components, with each component identified by its characteristic retention time and confirmed by mass spectrometry molecular-ion match against the empirical formulas reported on the COAs (C38H68N10O14 for TB-500; C62H98N16O22 for BPC-157). Purity is reported as combined HPLC-area composition on the blend's Certificate of Analysis. Peptide content where applicable is determined by amino-acid analysis or nitrogen-content assay following the analytical method specified on the COA. Residual solvent and water content are reported categorically when these parameters are part of the lot's release specification. The COA records the lot identifier, the relative amount of each component as supplied, the manufacturing date, and analytical method versions used. Researchers requiring component-level analytical detail should reference the component PDPs linked from the composition panel above.
For laboratory storage, the lyophilized blend should be held at −20°C in its sealed, light-protected container until ready for analytical use. Allow vials to equilibrate to ambient temperature before opening to avoid moisture condensation on the lyophile. Reconstitution for in-vitro experimental use is typically performed in bacteriostatic water or a researcher-selected buffer compatible with the downstream assay; once reconstituted, store the working solution at 2–8°C and characterize stability in the relevant buffer prior to extended storage. Combined-peptide blends may exhibit differential-stability behavior depending on the individual component chemistries — assay-specific stability characterization for each component is recommended. Avoid repeated freeze-thaw cycles of reconstituted material — single-use aliquots are preferred for experiments where blend composition stability is assay-critical. These handling parameters reflect general best-practice for combined lyophilized peptide reference materials and do not constitute preparation guidance for human or veterinary application.
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