Two research compounds aim at the same target and share almost nothing else. MID-35 is a 16-residue synthetic peptide of about 2.35 kDa with a decade of peer-reviewed academic work behind it and no clinical data at all. FLGR242 is an engineered follistatin construct sold since late 2025, described by its developer as a modified follistatin carrying an albumin-binding element, with no peer-reviewed record under that name.
This page compares them on evidence quality rather than on marketing claims. One rule governs it: every standard applied to one compound here is applied to the other in the same breath, at the same volume. Where the published record is thin on the Kimera side, this page says so in the same paragraph where it says so about the comparator. Kimera supplies MID-35 for laboratory research and does not sell FLGR242, which appears here for comparison only.
The shared target
Myostatin, also called growth differentiation factor 8, belongs to the TGF-beta superfamily and is the best-characterised negative regulator of skeletal-muscle mass. It binds activin type II receptors, which recruit type I receptors and phosphorylate Smad2/3. The activated complex suppresses the growth programme and switches on the atrophy-associated ubiquitin ligases Trim63 and Fbxo32. Animals carrying loss-of-function myostatin mutations show the double-muscled phenotype.
One species fact governs how far any rodent result travels. Latres and colleagues measured circulating ligand across species: myostatin runs 4 to 18-fold lower in monkeys, rats and humans than in mice, while activin A runs 3 to 4-fold higher in primates. Blocking myostatin alone with a neutralising antibody grew mouse tibialis anterior; in cynomolgus monkeys neither antibody alone did much and only the combination worked. Mice run on myostatin. Primates run on both.
Two caveats travel with that study. Mass was not force: in the same experiments mass rose by as much as about 49% while specific force did not change in any group. The declared conflict is also maximal and runs with the result. Every author was a company employee, and the company and five named authors hold patents on antibodies against both ligands. A finding that primates need both blocked argues for the combination those patents cover. It is the only cross-species measurement of its kind and it has not been independently reproduced.
MID-35: what has been measured
MID-35 is a 16-mer of 2350.99 Da, every residue in the D configuration, with the sequence order reversed relative to its parent. That is a retro-inverso design: reversing the order and inverting every stereocentre approximately reproduces the parent’s side-chain arrangement while presenting a backbone that mammalian proteases cleave poorly. The programme originated at Tokyo University of Pharmacy and Life Sciences with Fujita Health University, and the scaffold appears as SEQ ID NO: 22 in JP7740715B2, granted 17 September 2025.
Four peer-reviewed papers name the compound and report original mouse work. In a Smad-responsive reporter assay it produced fitted IC50 values of 0.19 µM against myostatin, 0.63 µM against GDF-11, 0.89 µM against activin A and 1.6 µM against TGF-beta-1. A single 30 nmol intramuscular injection into mouse tibialis anterior produced a treated muscle about 1.3 times the paired saline-injected control at day 28. A 2026 time course found differentiation markers up and atrophy markers down within three days, measurable weight gain from day 14, and a weight effect still present at day 84.
Three things about that record need stating plainly, because earlier versions of this page got them wrong.
The binding site is not known. No published study reports MID-35 binding by surface plasmon resonance, calorimetry, receptor competition, target occupancy, NMR, crystallography or hydrogen-deuterium exchange. Earlier versions of this page said MID-35 caps myostatin at its type I receptor interface, and named critical myostatin residues. Those claims belong to earlier 23- and 24-residue parent peptides, and to docking models of them. Retro-inversion plus two arginine substitutions prevent a one-to-one transfer onto MID-35. Pathway design makes direct receptor binding unlikely, but unlikely is not measured.
The parent potency figure is not a single number. The parent 23-mer has three measured IC50 values from one group: 4.1 µM in 2015, 3.53 µM in 2016, and 3.56 ± 0.25 µM in 2017. The later literature flattened them into one figure and in at least one case attributed it to the paper that printed a different value. The capped analogue downstream of it has three published values too.
The control designs are not uniform, and one result was overstated. Earlier versions of this page said every rodent study used the same internal control. That is false. Two studies used a contralateral saline-injected muscle in the same animal, one treated both legs and so has no untreated internal control, and one used separate control groups. The cancer-cachexia study’s survival comparison reached p = 0.052 against its own p < 0.05 threshold, so no significant survival benefit was established, and an earlier version of this page claimed one.
The evidence base is also narrow in ways worth saying out loud. Every published in vivo result comes from local delivery into a specific muscle, by direct injection or by iontophoresis into the tissue beneath the skin. Group sizes are commonly five or six animals. The author network overlaps across the whole lineage, and no independent laboratory has replicated the compound. No study has measured specific force, contractile function or endurance in a MID-35-treated animal. Full detail, including the corrections above, is in the MID-35 evidence review.
The lineage has its own failed systemic experiment
This is the part of the MID-35 record that a comparison page has the most duty to state, because it is the closest thing either compound has to a published systemic result.
The programme’s earlier 29-residue prodomain peptide was given intravenously by tail vein at 20 nmol, once weekly from 6 to 11 weeks of age. The animals were wild-type and caveolin 3-deficient mice, n = 5 as printed. The endpoints were body-weight gain and grip strength. It produced no effect on either. The same peptide given locally had worked. The authors offer two explanations in their own discussion. One is that the systemic dose may have been insufficient. The other is that the peptide may have been unstable against proteolysis when given intravenously. The experiment measured neither plasma concentration nor half-life nor biodistribution, so it cannot choose between them.
That is one dose, one schedule, two endpoints and no exposure measurement, so it is not evidence that systemic delivery of this chemistry cannot work. It is a published negative result, by the lineage’s own hands, on the route the comparator is designed for.
FLGR242: what is claimed, and what is public
FLGR242 starts from the opposite end. Rather than shrinking a natural inhibitor to its minimum, it engineers around one.
Follistatin is a secreted glycoprotein that binds and neutralises several TGF-beta superfamily ligands, myostatin among them, by sequestering the growth factor so it never reaches its receptor. The isoform naming matters here and an earlier version of this page had it backwards. FST-344 is the 344-residue precursor, which is processed to the circulating form FST-315. FST-288 lacks the acidic C-terminal tail, which leaves its heparin-binding site exposed, so it is the tissue-associated, pericellular form. FST-303 is a proteolytic clip of FST-315 rather than a third splice variant. Published surface-binding affinity ranks FST-288 above FST-303, above FST-315, above FSTL3. Writing “344 amino acids” as though it were a finished drug conflates a precursor with a product.
According to its developer, FLGR242 is a fragmented, modified version of FST-344 carrying two engineered features. The first is an alteration so that it no longer binds activin. The second is an albumin-binding element, described as a glycine-serine linker gripping serum albumin at sub-20 nM affinity, with a resulting half-life stated as up to roughly 19 days. The product is described as approximately 40 kDa and as a glycoprotein, though its lot certificates print the product type as “Peptides”.
What is genuinely public about the construct is narrow and specific. The albumin-binding sequence is published: a 29-mer consisting of a glycine-serine linker plus a core that matches the albumin-binding peptide SA21 described by Dennis and colleagues in 2002. That same sequence appears as SEQ ID NO: 4 in the body of US 12,377,158 B1. The abstract of that patent prints the string with a residue missing, so the body sequence is the one to read. The follistatin portion’s amino-acid sequence and domain boundaries are not public anywhere. No PubMed record, no Europe PMC record, no ClinicalTrials.gov registration and no patent uses the name FLGR242 or FLGR-242.
The accurate conclusion is not that there is nothing to find. Public material identifies the albumin-binding tag and contains a patent assertion of a seven-day canine half-life for an unnamed follistatin fusion, and the inventor of that linker has posted platform-level half-life figures for unnamed albumin-binding constructs. No public source supplies a myostatin-binding report for this construct, the complete construct sequence, or the claimed rodent, canine and swine study reports. The reported findings therefore cannot be independently checked.
The developer side states that private surface-plasmon-resonance binding work and animal studies exist and that release is conditioned on a further patent filing. That is a stated commitment with a named condition rather than a refusal, and it is not a report. Under the standard this page applies to both compounds, a claim about unreleased evidence is evidence of a claim, not evidence of a fact. It is also not disproved. The honest description is untestable rather than wrong.
The 19-day half-life, and what the class literature actually measured
Nineteen days is the textbook half-life of human serum albumin. Albumin binding is a clearance strategy, and it does not hand the cargo albumin’s own half-life: half-life is a property of the whole engineered molecule, not of the part that binds. No concentration-time study of this construct is public, so no half-life for it exists in the public record.
What the class literature measured, with species and cargo named, is a useful calibration.
| Source | Construct | Species and route | Measured half-life |
|---|---|---|---|
| Dennis 2002 | free SA21 peptide, 2 mg/kg | rabbit, intravenous | 2.31 ± 0.24 h |
| Dennis 2002 | Fab alone, then the same Fab with an albumin-binding peptide | rabbit | 0.88 h, then 32.4 ± 3.2 h |
| Dennis 2002 | Fab alone, then with the peptide | mouse | 0.40 h, then 10.4 h |
| Levy 2014 | SA21-loop cargo | rat, then monkey | 11 h; detectable 2 days |
| Levy 2014 | bacterial albumin-binding domain, same cargo | rat, then monkey | 16 h; more than 14 days |
| Tan 2020 | bacterial domain plus a peptide cargo | mouse | 31 to 38 h |
Dennis 2002 also measured SA21’s affinity for human albumin at 467 ± 47 nM. The sub-20 nM figure in the claim set comes from a later patent on the linker. The worked binding experiment in that patent measures native human albumin against a Klotho construct, not myostatin, and not on this product. A patent specification is a dated public claim about what was asserted and by when. It is not a measurement.
Dennis’s own mechanistic caution belongs here too: clearance of these constructs is faster than filtration of the calculated free fraction would predict, so metabolism rather than filtration accounts for most of the loss. Binding albumin does not stop the cargo being broken down.
The same arithmetic applies to the Kimera side of the page, and the answer is no better. MID-35 has no measured half-life in any species by any route. Its protease-resistance figures, 98.5 ± 7.8% and 97.0 ± 2.1% intact after 400 minutes with two isolated digestive enzymes, are stability measurements in buffer, not pharmacokinetics. A peptide fully resistant to serum proteases can still clear quickly through hepatic uptake or renal filtration. An earlier version of this page cited “14 days intact in human serum” for the parent series and claimed a net peptide content figure of 80 to 87% of vial mass. Neither is a lot-specific measurement of this compound and both have been removed.
The design points toward circulation, not toward muscle
There is a direction problem in the comparator’s story that is worth separating from the numbers. Heparan-sulfate binding is what holds follistatin on cell surfaces and pulls it out of blood. Removing that binding raises circulating exposure. Adding an albumin-binding tail slows clearance. Both edits are how a systemic agent is built.
The published class measurements run that way. An Fc fusion with a heparin-site edit reached a mouse intravenous half-life of 104 h, against native FST-315’s 1.2 h, with roughly 1600-fold higher exposure. A different heparin-site variant gave about 20-fold higher mouse exposure. The locally-acting designs did the opposite on purpose. They kept heparin binding on and were injected into the muscle. For the clinical example of that approach, intact drug was almost absent from serum after 24 hours. A construct described as heparin-reduced and albumin-tagged, and at the same time as muscle-directed with minimal systemic exposure, is being described in both directions at once. None of those measurements is a measurement of this product, and that is the point: the class evidence sets an expectation the product claims run against, and only a study of the product itself could settle it.
The follistatin precedent that most comparisons omit
A follistatin-based myostatin trap has already been through two randomised placebo-controlled phase 2 trials in humans.
ACE-083 is a modified human follistatin engineered as a local ligand trap. In a phase 1 study in healthy volunteers, injected muscle volume rose while strength did not, and serum drug was detectable in only 14 of 252 samples. Two phase 2 trials followed, one in facioscapulohumeral muscular dystrophy and one in Charcot-Marie-Tooth disease.
Both hit their muscle-volume endpoints convincingly. In the muscular dystrophy trial, treated muscle volume rose 14.20% against 5.46% for placebo in the lower limb and 20.41% against 1.07% in the upper arm, with isolated biceps strength rising 32.58% against a 3.54% decline. In the neuropathy trial, total muscle volume rose 13.5% over placebo and contractile volume 23.3%. Then every functional endpoint failed in both trials: walking distance, walk and run time, stair climb, upper-limb performance, quality of life and fall risk. Anti-drug antibodies appeared in 39.3% and 47.8% of treated patients. Both programmes were terminated.
ACE-083 is not FLGR242. It is a different construct with different engineering and a local rather than systemic design. It is the closest thing to a clinical readout that follistatin-based myostatin trapping has produced, and the readout was volume without function plus substantial immunogenicity. A recombinant protein carrying engineered non-native elements raises an immunogenicity question by construction. A synthetic 16-mer does not raise it in the same form, and it has not been tested for it either.
What a certificate of analysis can and cannot settle
Three lot certificates for the comparator are public. They establish that a vial was received, weighed and analysed, that the contents were not hot for endotoxin at the stated threshold, and that one dominant species eluted under the chromatographic conditions used. That is a lot-release screen. Several things it is not:
What the three certificates do not settle
- No molecular weight appears on any of the three. Not observed, not theoretical, not as a deviation. Each displays a raw mass spectrum as an image and then asserts that the identity is the product code. A figure that is displayed but never interpreted is not a result.
- The “determined identification” field restates the label. Mass spectrometry returns a mass, not a trade name. For a construct whose sequence is unpublished, mass spectrometry alone cannot establish identity at all: that needs a peptide map, amino-acid analysis, N-terminal sequencing or comparison against a reference standard. None appears.
- One certificate cannot settle the product’s own name. Its labelled and determined identity fields both read FLGR232, with a CAS number attached. The mass-spectrometry plot header on the same page reads FLGR242. A public search on that CAS number returned no structure and no follistatin record.
- Purity is a four-figure chromatographic area percent. Area percent cannot see water, counterion, buffer salts, residual solvent, or anything that does not elute. No quantitative NMR against a certified standard, no water determination, no residual solvent and no counterion figure appears on any of the three. Three lots received in different months all land within 0.08 percentage points of each other.
- Endotoxin is reported in units per millilitre for a dry solid. Without a reconstitution volume and tested concentration that unit does not convert. For a powder the release unit should be per milligram.
- One chromatogram excludes a large late-eluting region from its own integration. The integration baseline is drawn only beneath the main peak. The detector finishes the run at more than double the absorbance it started at, and none of that region is integrated. In fairness, at this wavelength in a reversed-phase gradient the baseline routinely drifts upward as organic increases. Some or all of that rise may be gradient rather than sample. No blank or gradient-only run is shown and no method is stated, so it cannot be called either way from what is printed. That is the problem.
- The annotated charge states do not deconvolute to a single mass. On one spectrum the labelled ions imply masses spread across roughly 6.8 kDa. On another they drift almost monotonically across about 2.9 kDa as the charge state falls. That drift is the signature of charge states assigned to the wrong peaks. Unlabelled peaks in the same spectrum sit near where a roughly 40 kDa species would place its ions. So the more likely reading is that a protein signal is present and the annotation is unreliable, rather than that nothing is there. Settling it needs the raw data files.
- One of the three has a clean chromatogram, with a flat baseline across the whole run and a return to the starting baseline, and it could plausibly support a high purity figure. That is stated because it is true and because the contrast is the point: the three lots are not equivalent and should not be described as though they were.
The same standard, applied to Kimera
Nothing above is an allegation that any measurement was fabricated or that the vial contains something other than what the label says. Identity is unconfirmed on these documents, which is a different and narrower statement than misidentification.
The same standard applies to Kimera. A certificate of analysis is lot release, not pharmacology, and that is as true of Kimera’s documents as of anyone else’s. HPLC purity reports the fraction of peptide-related material in the main peak and says nothing about how much peptide is in the vial. Substituting a D residue for an L residue does not change mass. So mass spectrometry alone cannot confirm that a D-peptide was built with the correct stereochemistry. Kimera’s answer is to publish lot documentation with multi-lab third-party verification in the COA archive. It is meant to be read off the certificate rather than off a catalogue page. A specification is not a measurement no matter whose page it sits on.
The one measurement offered on the comparator
A pre-and-post serum myostatin measurement from two individuals has been offered publicly, reporting a fall from a detectable value to below the assay’s limit of detection. Read generously, and generous is the correct reading here, that result is consistent with target engagement. It is not a clearance measurement and it is not an outcome. The kit named for it is described on its own product page as using an antibody pair validated for a different assay format, and not yet optimised for the one offered. Its published procedure also includes no dissociation step. That matters when a drug is bound to the analyte being measured. Two self-reported samples, with no control and no stated timing relative to dose, cannot answer the question in either direction. Asserting that the compound did not work would be the same overreach this page objects to.
Selectivity: mirror-image claims, one set of numbers
MID-35 is often labelled a selective myostatin inhibitor. Its own primary literature does not support that. The four fitted values span roughly eightfold, so a compound whose weakest measured target sits within an order of magnitude of its strongest is a broad TGF-beta family inhibitor with a preference. The activin A figure is also contested. A separate 2022 paper, using a different cell background at a single fixed concentration, reported no activin A inhibition. Its methods and figure caption disagree with each other on the activin concentration and the order of addition. The author groups overlap and no third measurement exists.
FLGR242’s central design claim is the mirror image: engineered specifically not to bind activin. No published dose-response data support it. The claim is plausible, because follistatin’s activin and myostatin binding surfaces are distinguishable and separating them is a recognised engineering goal, but plausible is not measured. The product page also lists activin neutralisation assays among its suggested research uses. That sits awkwardly beside a claim not to bind activin.
Read against the primate species data above, the two positions carry opposite implications. Activin-sparing selectivity is attractive on safety grounds and unattractive on efficacy grounds in primates, where activin A does much of the work. Broad blockade is the reverse. Neither compound has the data to settle which trade its design actually makes in a non-rodent species.
What the pathway itself costs, for either compound
Blocking myostatin reliably adds muscle mass. Whether the added mass performs is a separate question, and the answer applies to both compounds because it is a property of the pathway rather than of either molecule. None of the studies in this section used either compound.
In myostatin-null mice measured in vivo, gastrocnemius volume rose 118% while absolute force rose 34%. That is a large specific-force deficit. Four months of a soluble decoy receptor produced extreme muscle fatigability and a metabolic myopathy. Eight weeks of the same molecule, at the same dose and route, left fatigue resistance intact. But mitochondrial ATP-producing capacity was already dramatically reduced at that point. The shorter study is the early timepoint of the longer one, not a contradiction of it. The tidy fibre-type explanation for the cost is wrong. Overexpressing myostatin propeptide in adult mice caused fatigability and reduced exercise capacity with fibre-type distribution unchanged. That puts the cost in metabolism rather than typology. One construct deliberately traded the other way, buying endurance by curbing hypertrophy.
Two 2026 events frame the human side, and they point in opposite directions. An anti-latent-myostatin antibody was approved by the FDA on 11 September 2026 for spinal muscular atrophy in patients aged 2 and over, alongside existing SMN-targeted therapy, with a fracture-risk warning in its prescribing information. It is the first agent targeting myostatin approved for a muscle indication. Any claim that myostatin inhibition has never worked in humans is now out of date, including the narrower version that luspatercept is the only approval anywhere near this pathway.
In the other direction, a different anti-latent-myostatin antibody was discontinued in March 2026 across two neuromuscular indications. Its originator reported that the antibody showed target engagement by reducing mature myostatin, but that this did not translate into the intended functional outcomes. Target engagement is not efficacy and mass is not function, and both compounds on this page are measured against that bar rather than exempted from it.
Comparison at a glance
| Attribute | MID-35 | FLGR242 |
|---|---|---|
| Modality | Synthetic 16-mer retro-inverso all-D peptide | Recombinant engineered follistatin construct |
| Size | 2350.99 Da, sequence-derived | Approximately 40 kDa, developer-stated, absent from its own certificates |
| Parent | Mouse myostatin prodomain, via a 16-mer precursor | Described as a fragmented, modified FST-344 |
| Sequence in the public record | Full sequence published and matched to a granted patent example | Albumin-binding 29-mer published; follistatin portion not public |
| Mechanism | Binds the ligand rather than the receptor; exact interface unmeasured | Described as sequestering the ligand, as follistatin does; unmeasured on this construct |
| Selectivity | Measured and broad: GDF-11, activin A and TGF-beta-1 all within roughly eightfold. Activin A result contested | Claimed activin-sparing. No published dose-response |
| Stability strategy | D configuration and reversed backbone resist proteolysis in isolated-enzyme tests | Albumin binding intended to slow clearance |
| Measured half-life | None published, any species, any route | None published; roughly 19 days claimed, which is albumin’s own figure |
| Delivery in the evidence base | Local intramuscular and iontophoretic only. One published intravenous attempt in the lineage produced no effect | Designed for systemic exposure. No public exposure measurement |
| Production | Solid-phase synthesis, every residue and stereocentre specified | Recombinant expression plus modification, with glycosylation as a quality attribute |
| Glycosylation analysis | Not applicable | Central to the product claim, absent from all three certificates |
| Functional endpoints | No force, fatigue or endurance measurement in any species | No controlled functional measurement public |
| Immunogenicity | No data. Small synthetic peptide | No data. Recombinant protein with non-native elements |
| Independent replication | None | None |
| Human data | None | None |
What neither compound has
The similarities in the gaps are as informative as the differences in the designs.
- No human data. Neither has been administered to a human in any published or registered study.
- No published pharmacokinetics. No half-life, clearance or bioavailability in any species by any route, for either.
- No toxicology. No acute, repeat-dose, genotoxicity or safety pharmacology study for either. The only non-muscle tissue ever measured in a MID-35 study is heart weight relative to body weight, which was unchanged.
- No immunogenicity data for either, in any system.
- No validated bioanalytical assay for either in serum, plasma or urine, and none published for peptides of this class.
- No independent laboratory replication of either.
- No functional or strength endpoint demonstrated for either.
Follistatin biology carries one further open question, and it applies to the comparator’s class rather than to a short synthetic peptide. Follistatin overexpression has been associated with effects on bone, and the GDF-11 that these agents also block promotes osteogenesis. Neither compound has been evaluated on that endpoint. Adjacent compound profiles are collected in the peptides research library, and the receptor-side comparator in this pathway is ACE-031.
Frequently asked questions
What is the main difference between MID-35 and FLGR242?
Size and the shape of the evidence. MID-35 is a 2.35 kDa synthetic retro-inverso D-peptide. Its full sequence is published, and its mouse results appear in four peer-reviewed papers, all from local delivery. FLGR242 is a recombinant engineered follistatin construct characterised by its developer, with no peer-reviewed record under that name and no public construct sequence.
Do they work the same way?
Both are described as preventing myostatin from reaching its receptors rather than blocking the receptor. For MID-35 the binding surface has never been measured. For FLGR242 no binding measurement on the construct is public. Both mechanisms are inferences from the parent molecules they derive from.
Which one is more selective?
MID-35 measurably is not: its four published values sit within roughly eightfold, and its activin A result is disputed between two papers. FLGR242 claims activin-sparing selectivity with no published dose-response behind it. One side has numbers that undercut its own label. The other has a label with no numbers.
Why does MID-35 use D-amino acids?
Mammalian proteases cleave D-configured backbones poorly. A retro-inverso design reverses the sequence and inverts every stereocentre, which approximately preserves the side-chain arrangement while changing protease recognition. Piecemeal D-substitution was tried earlier in the programme and mostly reduced activity, which is why full retro-inversion was used.
Has anyone independently confirmed the 19-day half-life?
No. Nineteen days is the textbook half-life of human serum albumin. Albumin binding slows clearance but does not transfer albumin’s half-life to the cargo, and no concentration-time study of this construct is public. The measured class figures for albumin-binding constructs, named in the table above, run from hours to a few days in rodents.
Does MID-35 have a measured half-life?
No. Not in any species, by any route. Its protease-resistance figures are buffer measurements with isolated enzymes, which is a different property from elimination half-life.
Has a follistatin-based myostatin trap ever been tested in humans?
Yes. ACE-083 completed two randomised placebo-controlled phase 2 trials. Both significantly increased injected-muscle volume and both failed every functional endpoint, with anti-drug antibodies in 39.3% and 47.8% of treated patients. Both programmes were terminated. ACE-083 is a different construct from FLGR242, but it is the closest clinical readout the approach has produced.
Are the comparator’s private studies fake?
That is not the claim on this page. The claim is narrower and it is the only one the record supports: the reports have not been released, so they cannot be checked by anyone outside the company that holds them. Release has been stated to be conditioned on a further patent filing. Untestable is not the same as untrue.
Research use only
Kimera Chems supplies MID-35 strictly for laboratory research and analytical use. It is not a drug, food, cosmetic or dietary supplement, it is not for human or veterinary use, and it must not be administered to humans or animals. FLGR242 is discussed here for comparison and is not sold by Kimera. Nothing on this page describes or implies a therapeutic use, and no statement here has been evaluated by the FDA. Sales are limited to qualified research professionals and institutions.
References
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Sidis Y, Mukherjee A, Keutmann H, et al. Biological activity of follistatin isoforms and follistatin-like-3 is dependent on differential cell surface binding and specificity for activin, myostatin, and bone morphogenetic proteins. Endocrinology. 2006;147:3586-3597. doi:10.1210/en.2006-0089
Glasser CE, Gartner MR, Wilson D, Miller B, Sherman ML, Attie KM. Locally acting ACE-083 increases muscle volume in healthy volunteers. Muscle Nerve. 2018;57:921-926. doi:10.1002/mus.26113
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Thomas FP, Brannagan TH, Butterfield RJ, et al. Randomized phase 2 study of ACE-083 in patients with Charcot-Marie-Tooth disease. Neurology. 2022;98:e2356-e2367. doi:10.1212/WNL.0000000000200325
Latres E, Mastaitis J, Fury W, et al. Activin A more prominently regulates muscle mass in primates than does GDF8. Nat Commun. 2017;8:15153. doi:10.1038/ncomms15153
Giannesini B, Vilmen C, Amthor H, Bernard M, Bendahan D. Lack of myostatin impairs mechanical performance and ATP cost of contraction in exercising mouse gastrocnemius muscle in vivo. Am J Physiol Endocrinol Metab. 2013;305:E33-E40. doi:10.1152/ajpendo.00651.2012
Mouisel E, Relizani K, Mille-Hamard L, et al. Myostatin is a key mediator between energy metabolism and endurance capacity of skeletal muscle. Am J Physiol Regul Integr Comp Physiol. 2014;307:R444-R454. doi:10.1152/ajpregu.00377.2013
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Albumin binding peptides and fusion constructs. US 12,377,158 B1. Cited as a dated public claim, not as a measurement.
Peptides and complexes containing the same. JP7740715B2, granted 17 September 2025. SEQ ID NO: 22.
