ACE-031 1mg

ACE-031 Product Description

ACE-031 is described in primary literature as a soluble fusion protein combining the extracellular domain of activin receptor type IIB with a human IgG1 Fc region. This makes it a recombinant fusion construct, not a conventional short synthetic peptide. The supplied catalog record states 1 mg, but it does not identify construct boundaries, expression host, glycosylation, excipients, physical format, or lot-specific analytical properties.

The multi-ligand nature of ActRIIB-Fc is a critical interpretive boundary. Biochemical work reports binding to several TGF-beta-superfamily ligands, including GDF-8, GDF-11, and activin A. Describing ACE-031 as exclusively selective for one ligand would therefore oversimplify the cited evidence. Commercial naming alone also cannot prove equivalence to the recombinant construct studied in the literature.

The source set spans binding kinetics, C57BL/6 mouse experiments, and an early controlled single-ascending-dose study in healthy postmenopausal volunteers. These publications measured different layers of biology and should not be merged into a single performance narrative. The controlled participant study included pharmacokinetic, safety, and exploratory biomarker observations, but it does not validate this catalog material or support a use recommendation.

This page positions the item solely for qualified research into ligand trapping, receptor-domain interactions, and model-specific measurements. Experimental records should document the exact construct and preparation. Identity, content, purity, aggregation, glycosylation, sterility, endotoxin status, and stability remain unresolved until lot documentation is available. The catalog identity and the literature identity are recorded as separate evidence layers so that future documentation can resolve open attributes without rewriting the scientific history or overstating what the current source set demonstrates within defined research boundaries.

Research Material Profile

ACE-031 Research

Multi-ligand binding kinetics

A biochemical kinetics study used an ActRIIB-Fc chimera to compare interactions with several ligands, including GDF-8, GDF-11, and activin A. The measurements support a multi-ligand interpretation of the receptor-domain fusion and argue against presenting the studied construct as selectively myostatin-only. Binding kinetics are nevertheless assay-specific: immobilization strategy, analyte preparation, concentration range, and fitting model can influence reported parameters. The paper establishes research context for an ActRIIB-Fc construct characterized in that study, not the identity or binding profile of this 1 mg commercial item. Because the Lobo record does not state construct boundaries, expression host, or glycosylation, equivalence remains unresolved. The source is appropriately used to define the molecular class and to identify ligand-binding questions that researchers have examined. It does not support a claim that an untested lot will reproduce those measurements. (PubMed 20385559).

Mouse tissue and fiber measurements

In C57BL/6 mice, investigators examined soluble ActRIIB material identified as ACE-031 and measured tissue mass and fiber-level endpoints under the reported protocol. Those observations are restricted to the mouse model, construct preparation, experimental controls, and measurement methods used. They do not establish outcomes in another species and do not verify the material in this listing. The study is useful for understanding how a multi-ligand trap has been investigated beyond an isolated binding assay, but whole-animal measurements cannot reveal lot identity or prove selective engagement of only one ligand. A new research program should separate biochemical target engagement from tissue-level observations and characterize the exact fusion protein independently. This RUO summary avoids turning the model findings into a commercial promise and provides no operational or use guidance. (PubMed 20466801).

Controlled human research boundary

A single-ascending-dose study in healthy postmenopausal volunteers recorded pharmacokinetic, safety, and exploratory pharmacodynamic observations for ACE-031 in a controlled research context. The participant criteria and protocol define the scope of the findings. Exploratory endpoints are hypothesis-generating and should not be treated as established performance claims, while observations about the studied preparation do not establish the properties of a separately sourced RUO lot. The paper may inform critical review of which variables were monitored when an ActRIIB-Fc construct entered controlled human investigation. It does not resolve construct boundaries, expression system, glycosylation, aggregation, purity, or content for this catalog entry, and it supplies no basis for human or veterinary use. On this page, the study is cited only as model-qualified historical research context alongside biochemical and mouse evidence. (PubMed 23169607).

Evidence Boundaries

The cited literature supports only the identity and model-qualified research contexts summarized above for ACE-031. The label statement “1 mg” is preserved as supplied and is not treated as an analytical measurement. Study findings remain bounded by the reported biochemical assay, cell system, animal species, or controlled participant protocol. Lot-specific identity, content, purity, sterility, endotoxin status, stability, and other unreported specifications remain unknown unless separately documented. No procedural, operational, or outcome guidance is provided.

ACE-031 References

8 curated medical and scientific references used for identity, mechanism, model, and assay context.

1. Characterization of the ligand binding functionality of the extracellular domain of activin receptor type IIb.
   Dianne Sako, Asya V Grinberg, June Liu et al.. The Journal of biological chemistry. 2010.
   ingredient/parent context · Biochemical ligand-binding kinetics using an ActRIIB-Fc extracellular-domain construct
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2. Regulation of muscle growth by multiple ligands signaling through activin type II receptors.
   Se-Jin Lee, Lori A Reed, Monique V Davies et al.. Proceedings of the National Academy of Sciences of the United States of America. 2005.
   ingredient/parent context · Genetic and soluble-receptor experiments in mice
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3. Administration of a soluble activin type IIB receptor promotes skeletal muscle growth independent of fiber type.
   Samuel M Cadena, Kathleen N Tomkinson, Travis E Monnell et al.. Journal of applied physiology (Bethesda, Md. : 1985). 2010.
   exact identity · C57BL/6 mouse study of soluble ActRIIB material identified as ACE-031
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4. A single ascending-dose study of muscle regulator ACE-031 in healthy volunteers.
   Kenneth M Attie, Niels G Borgstein, Yijun Yang et al.. Muscle & nerve. 2013.
   exact identity · Randomized single-ascending-dose human study in healthy postmenopausal volunteers
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5. Myostatin inhibitor ACE-031 treatment of ambulatory boys with Duchenne muscular dystrophy: Results of a randomized, placebo-controlled clinical trial.
   Craig Campbell, Hugh J McMillan, Jean K Mah et al.. Muscle & nerve. 2017.
   exact identity · Randomized placebo-controlled human trial in ambulatory boys with Duchenne muscular dystrophy
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6. Gel Electrophoretic Detection of Black Market ACE-031.
   Christian Reichel, Thomas Filip, Günter Gmeiner et al.. Drug testing and analysis. 2025.
   method/assay context · Gel-electrophoretic analysis of black-market ACE-031 samples
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7. Combined detection of inhibitors of the activin receptor signaling pathways (IASPs) by means of LC-HRMS/MS for human doping control.
   Panagiotis Sakellariou, Katja Walpurgis, Andreas Thomas et al.. Scientific reports. 2025.
   method/assay context · Human doping-control LC-HRMS/MS method study
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8. ACE-031, a soluble activin type IIB receptor, increases muscle mass and strength in the common marmoset (Callithrix jacchus).
   Samuel M Cadena, Sasha Bogdanovich, Tejvir S Khurana et al.. PloS one. 2026.
   exact identity · Common-marmoset preclinical study
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