IGF-1 LR3 + BPC-157

1 Identity

Fixed-ratio two-component article: an 83-residue recombinant single-chain protein with three intramolecular disulfides, co-lyophilized with a 15-residue all-L synthetic peptide free acid. and "Long R3 IGF-1 with BPC-157". "Long R3 IGF-1" and "IGF-1 LR3" are the same construct; "IGF-1 des" is a different molecule and a separate record.

Sequence

Per component, cross-referenced rather than restated. IGF-1 LR3: a 13-residue N-terminal leader fused to human IGF-1(1-70) carrying Glu3Arg, 83 residues in all, so the mature segment begins GPR- and not GPE-, which is the fastest visual check available on a declared sequence. Six cysteines, three disulfides: Cys19-Cys61, Cys60-Cys65 and Cys31-Cys74 in 83-residue numbering. BPC-157: H-GEPPPGKPADDAGLV-OH, free acid, no cysteine, no aromatic residue and therefore no 280 nm chromophore of its own; four prolines, at positions 3, 4, 5 and 8, make cis/trans isomerism a chromatographic feature of the peak shape rather than an impurity to be chased.

Molecular formula

Per component; a mixture has no combined formula and none is written. IGF-1 LR3 C400H619N111O115S9 with all three disulfides formed, C400H625N111O115S9 fully reduced. BPC-157 C62H98N16O22. Counterion is a measured finding per component and the two components are unlike in this: the protein is supplied as a lyophilized free base or in an acetate-buffered matrix rather than as a simple peptide salt, and the 15-mer most often as a trifluoroacetate.

Average mass

Per component. IGF-1 LR3 9,111.55 Da oxidized and 9,117.60 Da fully reduced — the 6.05 Da gap is the arithmetic that proves three disulfides are formed, and it is the only mass evidence of folding available. BPC-157 1,419.556 Da. AT A nominal 1 mg plus 10 mg fill, 11 mg total, the 1.0-to-10.0 mass ratio is a molar ratio of 1.00 to 64.19, that is 0.10975 against 7.04446 micromol. That is the most extreme molar disparity of any blend in this group, a 6.4-fold mass difference multiplied by a 10-fold fill difference, and it is stated because trade documents describe such fills as combinations of equals rather than as one component with a small quantity of another.

Monoisotopic mass

Per component, and monoisotopic is not the release measurement on the protein. IGF-1 LR3 9,105.3487 oxidized and 9,111.3957 fully reduced, quoted as reference values only: at 9 kDa the monoisotopic peak is not the base peak of the isotope envelope, so a usable certificate reports a deconvoluted average mass with the charge-state series printed. BPC-157 1,418.7042 neutral, [M+H]+ 1,419.7115. The mass test the protein defeats: scrambled-disulfide isomers are exactly isobaric with correctly folded material and frequently co-elute on reversed phase, so no mass figure at any resolution distinguishes them, and only peptide-map disulfide connectivity does.

Salt / variant note

Scrambled-disulfide isomers of the protein are the principal quality variable in refolded material: exactly isobaric, frequently co-eluting, and invisible to mass and RP-HPLC alike. The fully reduced protein sits at +6.05 Da average. The construct fork: IGF-1 LR3 at 83 residues against IGF-1 des(1-3) and against native IGF-1(1-70), all three circulating in this category and all three different molecules, with the GPE- against GPR- mature N-terminus as the check. Native recombinant human IGF-1 is the active moiety of an approved United States product marketed as Increlex, whose drug substance is mecasermin — a different construct from the 83-residue LR3 fusion, and the two names are not interchangeable as identity. BPC-157 salt forms, the acetate and the arginate, are separate records with different gross weights. Counterion and residual-moisture state are stated per component. Ratio: 1 mg plus 10 mg is a stated nominal and no ratio for this article is standard.

2 Class & testing panel

Form

Fixed-ratio blend

Testing panel

P4 and P1 — panel definitionas a union, not the higher of the two, each panel run on the component it governs rather than once on the blended vial. P4 governs the protein and brings attributes no peptide panel carries: disulfide connectivity mapping, host-cell protein, host-cell DNA, endotoxin, aggregate content by SEC, and an expression-host declaration. P1 governs the 15-mer. Neither component contains a D-residue or a non-proteinogenic residue, so no chiral limit applies and a chiral method added here would be a method copied from a neighboring record. One deconvolution problem is specific to this pairing and is stated rather than hidden: BPC-157's composition is a strict subset of the protein's, so it has no unique marker residue at all, its net content is obtainable only by difference on proline, and the certificate prints that seven-per-mole-plus-four-per-mole arithmetic rather than reporting a number whose provenance is invisible

3 Primary sources & evidence

The index reports the design and provenance of the literature, not a conclusion about effect.

Published literature exists for each component, is graded on that component's record and is cross-referenced from here rather than restated. The protein component's literature is unusual in this catalog for resting substantially on cell-culture and bioprocess work rather than on animal studies. No published study of this fixed two-component combination at any ratio was located.

4 Storage & specification

Storage

Co-lyophilized solid in Type I amber glass, stored at -20 degrees C plus or minus 5 degrees C, desiccated and protected from light. Non-sterile, with no sterility claim. The protein governs every handling rule on this article: repeated freeze-thaw is the aggregation pathway, so the article is subdivided once on receipt rather than returned to the freezer as a stock solution; the disulfide set is the redox-sensitive feature, so nitrogen headspace is a written condition rather than a preference; and the reconstitution buffer, its pH and any surfactant are named on the label rather than left to the user.

Shelf life

Provisional 24 months at -20 degrees C plus or minus 5 degrees C, desiccated and protected from light, from the date of QA release, with a mandatory interim pull on each of the first three lots. The retest-limiting attributes are protein attributes rather than peptide attributes — aggregate content by SEC, disulfide scrambling by non-reduced peptide map, and deamidation at the protein's asparagine and glutamine positions — because the 15-mer carries no cysteine, no methionine and no aromatic residue and therefore has no oxidation pathway to run. Per-component net content and the measured ratio are carried at every pull.