PRODUCTS SOLD ON PEPTIDESLABIRELAND.COM ARE FOR RESEARCH PURPOSES ONLY AND ARE NOT FOR HUMAN OR VETERINARY USE.
PRODUCTS SOLD ON PEPTIDESLABIRELAND.COM ARE FOR RESEARCH PURPOSES ONLY AND ARE NOT FOR HUMAN OR VETERINARY USE.
€92.00
ACE-031 Ireland – Buy Online | In Stock & Ready to Ship
Buy ACE-031 in Ireland with fast shipping and guaranteed ≥99% purity — verified with COA and HPLC documentation. A trusted choice for peptides Ireland research teams rely on, with no customs delays or international wait times. Whether you’re searching for ACE-031 Ireland suppliers or looking to buy peptides Ireland-wide, we have you covered. Irish research teams can count on consistent stock, rapid fulfilment and full batch documentation every time.
For research use only. Not intended for human or veterinary use.
ACE-031 is a synthetic recombinant fusion protein and one of the most pharmacologically potent and mechanistically distinctive muscle mass regulatory research compounds available to laboratories in Ireland — a soluble decoy receptor constructed by fusing the extracellular ligand-binding domain of activin receptor type IIB (ActRIIB) to the Fc region of human IgG1, engineered to sequester myostatin, activin A, GDF-11, and multiple other ActRIIB ligands from their endogenous receptors with high affinity and prolonged plasma half-life, producing profound and sustained skeletal muscle hypertrophy, bone density increases, and fat mass reduction through pan-ActRIIB ligand neutralisation, making it an indispensable research tool for studying the complete ActRIIB ligand biology and its collective contribution to muscle mass regulation, dissecting the individual versus combined contributions of myostatin, activin A, and GDF-11 to skeletal muscle atrophy, characterising the downstream consequences of pan-ActRIIB pathway suppression on Smad2/3 signalling and muscle anabolic biology, investigating the musculoskeletal and metabolic consequences of broad TGF-beta superfamily inhibition, and modelling the pharmacological biology relevant to muscle wasting disease intervention in cachexia, sarcopenia, muscular dystrophy, and neuromuscular disease research. Researchers and institutions across Ireland can source verified, research-grade ACE-031 directly from our Irish peptide and protein supply, with domestic-speed dispatch and complete batch documentation.
✅ ≥99% Purity — HPLC & Mass Spectrometry Verified
✅ Batch-Specific Certificate of Analysis (CoA) Included
✅ Sterile Lyophilised Powder | GMP Manufactured
✅ Fast Dispatch to Ireland | Peptides Ireland Stock
ACE-031 is a recombinant fusion protein developed by Acceleron Pharma — comprising the extracellular ligand-binding domain of human ActRIIB fused to the Fc region of human immunoglobulin G1 — engineered as a soluble decoy receptor that competes with cell-surface ActRIIB for ligand binding in the extracellular space, sequestering ActRIIB ligands including myostatin (GDF-8), activin A, GDF-11, BMP-9, and BMP-10 before they can engage the signalling receptor and activate the downstream Smad2/3 atrophy pathway. The compound belongs to the class of Fc-fusion trap proteins — a well-established recombinant protein engineering strategy that exploits the Fc region’s capacity for neonatal Fc receptor-mediated recycling to extend the plasma half-life of the fused binding domain far beyond what the extracellular domain alone would achieve — producing a pharmacokinetic profile suitable for infrequent dosing in pre-clinical research and enabling sustained ActRIIB ligand neutralisation that produces the progressive and maintained muscle hypertrophy that distinguishes ACE-031 from shorter-acting inhibitory approaches.
The design rationale for ACE-031 as a research compound reflects a fundamental insight into the biology of muscle mass regulation — that skeletal muscle mass is negatively regulated not by a single ligand but by multiple TGF-beta superfamily members that converge on ActRIIB as their shared high-affinity receptor, and that comprehensive relief of this negative regulatory burden requires simultaneous neutralisation of all ActRIIB ligands rather than selective inhibition of any single one. Myostatin-selective inhibitors — anti-myostatin antibodies, myostatin propeptide, and myostatin-selective small molecule approaches — produce meaningful but submaximal muscle hypertrophy, reflecting the fact that activin A, GDF-11, and other ActRIIB ligands continue to suppress muscle growth even when myostatin is specifically neutralised. ACE-031’s pan-ActRIIB ligand trapping produces muscle hypertrophy substantially exceeding that achieved by myostatin-selective inhibition alone — establishing that the collective ActRIIB ligand burden is the biologically relevant target for maximal muscle mass augmentation and making ACE-031 the reference research tool for studying the complete ActRIIB pathway biology.
ACE-031 has been studied both as a pharmacological research tool for dissecting ActRIIB ligand biology and as a pre-clinical and early clinical stage muscle wasting disease intervention compound — with clinical studies in Duchenne muscular dystrophy and healthy volunteers characterising ACE-031’s muscle hypertrophic and bone anabolic effects in humans before the clinical programme was discontinued following telangiectasia and epistaxis adverse events at higher doses, findings that have themselves become important data points in understanding the biology of broad TGF-beta superfamily inhibition and the role of BMP-9 and BMP-10 neutralisation in vascular biology.
In controlled laboratory and pre-clinical settings, ACE-031 is studied across a range of ActRIIB ligand biology, pan-TGF-beta superfamily inhibition, skeletal muscle hypertrophy, muscle wasting disease, bone biology, and metabolic research applications:
ACE-031 is the primary research tool for studying the complete spectrum of ActRIIB ligand biology — enabling simultaneous neutralisation of all ActRIIB-binding TGF-beta superfamily members to characterise the collective biological consequences of pan-ActRIIB ligand withdrawal. Research has used ACE-031 to examine the relative contributions of individual ActRIIB ligands — myostatin, activin A, GDF-11, and others — to baseline muscle mass regulation by comparing ACE-031’s effects with those of ligand-selective inhibitors that neutralise only one family member at a time. Studies have characterised the binding affinities of ACE-031’s ActRIIB extracellular domain for each of its known ligands — establishing the rank order of ligand binding affinity and the stoichiometry of ligand neutralisation at physiologically relevant concentrations. These pan-ActRIIB ligand biology studies have been fundamental to establishing that skeletal muscle mass regulation is a multi-ligand system and that the full hypertrophic potential accessible through ActRIIB pathway blockade can only be realised by neutralising the complete ActRIIB ligand ensemble rather than individual members selectively.
ACE-031 is used in direct comparative research with myostatin-selective inhibitors — examining how the muscle hypertrophy, bone anabolic, and metabolic effects of pan-ActRIIB ligand neutralisation compare with myostatin-selective antibody or propeptide-based inhibition at equivalent doses and treatment durations. Research has characterised the incremental muscle hypertrophy attributable to neutralising activin A and GDF-11 in addition to myostatin — by comparing ACE-031-treated and myostatin-selective inhibitor-treated animals at matched experimental conditions and attributing the difference in muscle hypertrophic response to the additional ActRIIB ligands neutralised by ACE-031 but not by the myostatin-selective comparator. These comparative inhibition studies have established the relative importance of each ActRIIB ligand to the total negative regulatory burden on skeletal muscle mass and have contributed to understanding of why pan-ActRIIB ligand neutralisation produces superior muscle anabolic effects relative to myostatin-selective approaches.
ACE-031 produces the most profound pharmacologically induced skeletal muscle hypertrophy achievable through TGF-beta superfamily inhibition — and research has characterised the cellular and molecular basis of this hypertrophic response in detail. Studies have examined whether ACE-031-induced muscle hypertrophy proceeds through muscle fibre hypertrophy, hyperplasia, or both — characterising fibre size distribution changes, myonuclear accretion through satellite cell fusion, and fibre type composition shifts in ACE-031-treated muscle. Research has characterised the downstream molecular consequences of pan-ActRIIB ligand neutralisation on anabolic signalling in muscle — documenting de-repression of the IGF-1/PI3K/Akt/mTOR protein synthesis pathway that is chronically suppressed by ActRIIB ligand-Smad2/3 signalling, downregulation of MuRF1 and atrogin-1 ubiquitin ligase expression, and activation of the myogenic programme through relieved MyoD and myogenin suppression. These muscle hypertrophy mechanism studies have established the complete molecular programme through which pan-ActRIIB ligand neutralisation produces muscle mass increase and provided the framework for understanding how the removal of multiple convergent inhibitory signals produces a hypertrophic response exceeding that achievable by relieving any single inhibitory input.
Pan-ActRIIB ligand neutralisation with ACE-031 relieves the multiple myostatin- and activin-mediated inhibitory inputs that maintain satellite cells in quiescence and suppress their proliferative and differentiation responses to muscle injury — producing satellite cell pool expansion and enhanced muscle regenerative capacity that makes ACE-031 a research tool for studying the biology of satellite cell activation under conditions of maximal ActRIIB pathway de-repression. Research has characterised ACE-031’s effects on satellite cell number, activation state, and differentiation capacity in normal and injured muscle — examining how simultaneous relief of myostatin and activin A inhibition influences satellite cell biology relative to myostatin-selective inhibition alone. Studies have used ACE-031 in muscle injury and regeneration models to characterise whether pan-ActRIIB ligand neutralisation enhances regenerative efficiency — measuring myofibre regeneration kinetics, satellite cell contribution to repair, and functional recovery following injury as endpoints for satellite cell biology characterisation. These regeneration studies have contributed to understanding of how the combined myostatin-activin inhibitory burden on satellite cells limits muscle regenerative capacity and how comprehensive ActRIIB pathway de-repression could potentially enhance regenerative outcomes in muscle wasting diseases characterised by failed regeneration.
ACE-031’s potent muscle anabolic effects have made it a primary research tool for studying muscle wasting disease biology and evaluating pan-ActRIIB ligand neutralisation as a therapeutic strategy in pre-clinical disease models. Research has examined ACE-031’s capacity to prevent or reverse muscle wasting in cachexia models — including cancer cachexia models where tumour-derived factors including activin A drive profound muscle atrophy through ActRIIB activation — with studies characterising the degree of muscle mass preservation and functional improvement achievable with ACE-031 treatment in tumour-bearing animals. In muscular dystrophy models — particularly the mdx mouse model of Duchenne muscular dystrophy — research has examined whether ACE-031-induced muscle hypertrophy and enhanced regeneration can compensate for the ongoing muscle fibre necrosis caused by dystrophin deficiency and improve functional outcomes in this disease context. Sarcopenia models examining age-related muscle wasting have used ACE-031 to determine the contribution of elevated ActRIIB ligand signalling to age-associated muscle loss and the degree of muscle mass restoration achievable through pan-ActRIIB ligand neutralisation in aged animals. These disease model studies have collectively established ACE-031 as the reference tool for maximal ActRIIB pathway inhibition in pre-clinical muscle wasting research.
ACE-031’s muscle hypertrophic effects are accompanied by significant bone anabolic effects — with research characterising ACE-031-induced increases in bone mineral density, bone volume, and bone strength in pre-clinical models that reflect both the secondary mechanical loading effects of increased muscle mass on adjacent bone and direct ActRIIB ligand neutralisation effects on bone cell biology. Research has characterised ACE-031’s effects on osteoblast and osteoclast biology — examining how neutralisation of ActRIIB ligands including activin A and GDF-11 in bone tissue influences bone formation and resorption, trabecular and cortical bone architecture, and bone turnover marker expression. Studies have examined whether ACE-031’s bone anabolic effects are mechanically driven — through increased muscle force on bone — or direct — through ActRIIB ligand neutralisation in bone cells — by examining bone biology in immobilised and normally loaded animal models treated with ACE-031. These musculoskeletal biology studies have contributed to understanding of the integrated mechanical and paracrine coupling between muscle and bone and the potential of ActRIIB pathway inhibition for addressing the concurrent muscle and bone loss that characterises sarco-osteoporosis in ageing and disease.
ACE-031’s neutralisation of activin A — a TGF-beta superfamily member with important muscle regulatory, reproductive, immune, and cancer biology — provides a research tool for studying activin A’s contribution to muscle mass regulation in the context of pan-ActRIIB inhibition. Research has used ACE-031 in combination with myostatin-selective inhibitors to dissect the specific contribution of activin A neutralisation — beyond myostatin inhibition — to muscle hypertrophy, examining the incremental muscle anabolic effect attributable to blocking activin A through ActRIIB relative to myostatin-selective blockade. Studies have examined the relevance of activin A as an ActRIIB ligand in cachexia biology — where tumour-derived activin A has been specifically characterised as a driver of cancer cachexia muscle wasting through ActRIIB activation — and have used ACE-031’s activin A neutralisation capacity to study this biology in tumour-bearing animal models. These activin A biology studies have established ACE-031 as a research tool for examining the multi-ligand complexity of ActRIIB-mediated muscle regulation and the specific contribution of non-myostatin ActRIIB ligands to muscle wasting in different disease contexts.
Pan-ActRIIB ligand neutralisation with ACE-031 produces not only skeletal muscle hypertrophy but also significant fat mass reduction — and research has characterised the metabolic mechanisms through which ActRIIB ligand neutralisation influences adipose tissue biology and systemic energy metabolism. Studies have examined whether ACE-031-induced fat mass reduction reflects increased energy expenditure from expanded metabolically active skeletal muscle mass, direct ActRIIB ligand effects on adipocyte differentiation and lipolysis, or both — characterising the metabolic rate, substrate utilisation, and adipose tissue biology changes accompanying ACE-031-induced body composition improvements. Research has documented improvements in insulin sensitivity, glucose tolerance, and metabolic parameters following ACE-031 treatment in obese and metabolic disease models — contributing to understanding of how pan-ActRIIB ligand neutralisation produces metabolic benefits through the interaction between muscle mass expansion, fat mass reduction, and improved insulin-stimulated glucose disposal. These metabolic biology studies have extended ACE-031’s research significance beyond muscle wasting disease to encompass metabolic syndrome and obesity biology.
The clinical observation of telangiectasia and epistaxis in ACE-031-treated human subjects — findings that contributed to discontinuation of the clinical programme — identified an important and unexpected dimension of pan-ActRIIB ligand neutralisation biology that has become a significant research focus. BMP-9 and BMP-10 — bone morphogenetic proteins that signal through ActRIIB and related receptors — are critical regulators of vascular endothelial quiescence and vascular integrity, maintaining the endothelial cell quiescent phenotype through ALK1-mediated signalling that is disrupted when BMP-9 and BMP-10 are neutralised by the ActRIIB extracellular domain in ACE-031. Research has examined the vascular biology consequences of BMP-9 and BMP-10 neutralisation — characterising the endothelial cell biology, angiogenic signalling, and vascular remodelling that occur when these vascular stability signals are blocked, and investigating whether the telangiectasia and bleeding complications observed clinically reflect the same BMP-9/BMP-10 vascular biology mechanism characterised in pre-clinical vascular biology studies. These vascular biology studies have established that the ActRIIB ligand spectrum neutralised by ACE-031 includes not only muscle regulatory ligands but also vascular regulatory BMPs — providing important safety biology insights relevant to the design of next-generation ActRIIB-targeted research compounds with improved vascular safety profiles.
Pre-clinical research has documented ACE-031’s capacity to produce skeletal muscle hypertrophy substantially exceeding that achieved by myostatin-selective inhibition — with studies in rodent models characterising dose-dependent muscle mass increases of 15–30% or greater following ACE-031 treatment and demonstrating that these gains exceed those of myostatin antibody-treated animals at equivalent treatment durations. These comparative hypertrophy studies established the fundamental research finding that pan-ActRIIB ligand neutralisation produces superior muscle anabolic effects relative to myostatin-selective inhibition — validating the multi-ligand inhibition hypothesis and establishing ACE-031 as the reference compound for maximal pharmacological muscle hypertrophy in pre-clinical research.
Research using ACE-031 in combination with myostatin-selective inhibitors has established activin A as the primary non-myostatin ActRIIB ligand contributing to muscle mass regulation — with studies characterising that the incremental muscle hypertrophy achievable by switching from myostatin-selective to pan-ActRIIB inhibition is substantially attributable to activin A neutralisation. These activin A contribution studies have been important for understanding why pan-ActRIIB inhibition with ACE-031 exceeds myostatin-selective approaches and have identified activin A as an independent muscle mass regulatory signal whose contribution to the total ActRIIB inhibitory burden is comparable in magnitude to myostatin in certain physiological and disease contexts.
Research has documented reversal of cancer cachexia-associated muscle wasting following ACE-031 treatment in pre-clinical tumour-bearing animal models — with studies characterising significant muscle mass preservation, attenuation of body weight loss, and in some models extended survival in ACE-031-treated tumour-bearing animals relative to vehicle-treated controls. Mechanistic studies have identified tumour-derived activin A as a primary driver of cancer cachexia muscle wasting through ActRIIB activation — establishing that ACE-031’s neutralisation of both tumour-derived activin A and myostatin is required for optimal muscle mass preservation in cancer cachexia models and contributing to understanding of the multi-ligand ActRIIB pathway activation that underlies cancer-associated muscle wasting.
Research has documented significant increases in bone mineral density, trabecular bone volume, and bone mechanical strength following ACE-031 treatment in pre-clinical models — with studies characterising both the magnitude of bone anabolic effects and the relative contributions of direct ActRIIB ligand neutralisation in bone tissue versus secondary mechanical loading effects from increased muscle mass. These bone biology studies established ACE-031 as producing concurrent musculoskeletal anabolic effects in both muscle and bone — contributing to research interest in ActRIIB pathway inhibition for the concurrent muscle and bone loss that characterises ageing-associated sarco-osteoporosis.
Phase 1 and Phase 2 clinical research documented ACE-031’s muscle hypertrophic and bone anabolic effects in human subjects — with studies in healthy postmenopausal women and Duchenne muscular dystrophy patients characterising dose-dependent increases in lean mass, decreases in fat mass, and increases in bone turnover markers consistent with bone anabolic activity. These clinical studies provided important translational validation of the pre-clinical biology — confirming that pan-ActRIIB ligand neutralisation produces meaningful and dose-dependent muscle and bone anabolic effects in humans — while also documenting the telangiectasia and epistaxis findings that informed understanding of the vascular biology consequences of broad ActRIIB ligand neutralisation including BMP-9/BMP-10.
Research has characterised the downstream molecular consequences of ACE-031-mediated pan-ActRIIB ligand neutralisation — documenting suppression of Smad2/3 phosphorylation in skeletal muscle, downregulation of MuRF1 and atrogin-1 atrophy gene expression, de-repression of IGF-1/Akt/mTOR anabolic signalling, and restoration of myogenic regulatory factor activity in ACE-031-treated muscle. These signal transduction studies established the molecular basis for ACE-031-induced muscle hypertrophy at the level of the ActRIIB-Smad2/3 pathway and provided mechanistic confirmation that ACE-031’s muscle anabolic effects proceed through relief of the convergent Smad2/3-mediated inhibitory programme rather than through alternative signalling mechanisms.
Research has examined ACE-031’s effects in the mdx mouse model of Duchenne muscular dystrophy — documenting muscle mass increases, improved muscle function, reduced fibrosis, and enhanced regenerative efficiency in ACE-031-treated dystrophic animals. Clinical Phase 2 research in DMD patients characterised ACE-031’s lean mass-increasing effects in this patient population — providing translational evidence for the muscle anabolic biology in a human disease context and contributing important data on ACE-031’s biological effects in dystrophin-deficient muscle alongside the safety observations that informed the programme’s subsequent clinical direction.
| Feature | ACE-031 | GDF-8 (Myostatin) | Anti-Myostatin Antibody | Follistatin | Activin A |
|---|---|---|---|---|---|
| Type | Soluble ActRIIB-Fc decoy receptor fusion protein | Recombinant ActRIIB ligand — myostatin | Myostatin-selective monoclonal antibody | Endogenous pan-ActRIIB ligand inhibitor protein | Recombinant ActRIIB ligand — activin |
| Mechanism | Pan-ActRIIB ligand sequestration — neutralises myostatin, activin A, GDF-11, BMP-9, BMP-10 and other ActRIIB ligands | ActRIIB/ALK4/ALK5 agonism — activates Smad2/3 atrophy programme | Myostatin-selective neutralisation — prevents GDF-8 ActRIIB engagement only | Binds and neutralises myostatin, activins, and other TGF-beta superfamily members with varying affinity | ActRIIB/ALK4/ALK7 agonism — activates Smad2/3; contributes to muscle wasting and reproductive regulation |
| Ligand Selectivity | Pan-ActRIIB — multiple ligands neutralised simultaneously | Single ligand — myostatin agonist | Myostatin-selective | Broad — myostatin, activins, some BMPs | Single ligand — activin A agonist |
| Effect on Muscle Mass | Profoundly anabolic — greatest pharmacological muscle hypertrophy achievable through TGF-beta superfamily inhibition | Catabolic — activates full muscle atrophy programme | Moderately anabolic — myostatin-selective relief of growth inhibition | Anabolic — broader than myostatin-selective antibody | Catabolic — muscle wasting through ActRIIB-Smad2/3 |
| Bone Effects | Anabolic — increases bone mineral density and bone strength | Catabolic indirectly — muscle loss reduces bone loading | Mildly anabolic | Anabolic | Variable |
| Vascular Biology | BMP-9/BMP-10 neutralisation — telangiectasia risk at higher doses | Minimal direct vascular effects | Minimal | Minimal | Pro-angiogenic in some contexts |
| Half-Life | Extended — IgG1 Fc-mediated neonatal FcR recycling | Short — hours without carrier protein | Extended — IgG half-life | Short — hours | Short |
| Key Research Application | Pan-ActRIIB ligand biology / maximal muscle hypertrophy model / muscle wasting disease / comparative inhibition studies | Muscle atrophy biology / ActRIIB pharmacology reference agonist / inhibitor screening | Myostatin-selective inhibition / comparative biology with ACE-031 | Endogenous inhibitor biology / muscle hypertrophy | Cancer cachexia / reproductive biology / immune regulation |
| Research Profile | Extensively studied — reference pan-ActRIIB inhibitor | Extensively studied — reference ActRIIB agonist | Extensively studied | Extensively studied | Extensively studied |
| Parameter | Detail |
|---|---|
| Name | ACE-031 |
| Full Designation | Soluble ActRIIB Extracellular Domain — Human IgG1 Fc Fusion Protein |
| Also Designated | ActRIIB-Fc / sActRIIB-Fc / ACVR2B-Fc |
| Type | Recombinant Fc-Fusion Decoy Receptor Protein — Research Grade |
| Structure | ActRIIB extracellular ligand-binding domain (amino acids 1–131) fused via linker to human IgG1 Fc region — expressed as disulfide-linked homodimer |
| Molecular Weight | ~60–80 kDa (homodimer, glycosylated) |
| Mechanism | Extracellular sequestration of ActRIIB ligands — myostatin (GDF-8), activin A, GDF-11, BMP-9, BMP-10, and other TGF-beta superfamily members → prevents ActRIIB receptor engagement → blocks Smad2/3 activation → relieves muscle atrophy programme → skeletal muscle hypertrophy, bone anabolic effects, fat mass reduction |
| Ligands Neutralised | GDF-8 (myostatin) / Activin A / GDF-11 / BMP-9 / BMP-10 / additional ActRIIB-binding TGF-beta superfamily members |
| Key Research Distinction | Only pan-ActRIIB ligand trap producing simultaneous neutralisation of all ActRIIB ligands — reference compound for maximal pharmacological muscle hypertrophy and comparative ActRIIB ligand biology |
| Primary Research Areas | Pan-ActRIIB ligand biology / skeletal muscle hypertrophy / muscle wasting disease / satellite cell biology / bone anabolic biology / cancer cachexia / metabolic disease / vascular BMP biology |
| Vascular Biology Note | BMP-9/BMP-10 neutralisation — telangiectasia and vascular biology effects documented at higher doses in clinical studies; relevant for in vivo research design |
| Purity | ≥99% HPLC & MS Verified |
| Form | Sterile Lyophilised Powder |
| Solubility | Sterile PBS — see reconstitution note |
| Storage (Powder) | -20°C, protect from light and moisture |
| Storage (Reconstituted) | -80°C in aliquots with carrier protein — minimise freeze-thaw cycles |
| Manufacturing | GMP Manufactured |
| Intended Use | Research use only |
ACE-031 is a recombinant glycosylated Fc-fusion protein whose biological activity depends on the intact ActRIIB extracellular domain fold, the correct disulfide bonding within both the ActRIIB domain and the IgG1 Fc region, and the homodimeric quaternary structure maintained by Fc region disulfide linkage — reconstitution and handling conditions must preserve this protein architecture to maintain ActRIIB ligand binding affinity and the extended half-life properties conferred by intact Fc region structure. For standard reconstitution, add sterile phosphate-buffered saline slowly to the lyophilised powder and swirl gently until dissolved — do not vortex or agitate vigorously, as mechanical disruption promotes protein aggregation and can compromise Fc domain integrity. Reconstitution in PBS at neutral pH is preferred for Fc-fusion proteins as it maintains the native protein conformation and Fc structural integrity.
Carrier protein supplementation is strongly recommended for ACE-031 working solutions at lower concentrations — prepare working dilutions in PBS or cell culture media supplemented with 0.1% BSA to minimise surface adsorption losses and prevent protein aggregation at nanomolar working concentrations typical of ActRIIB ligand binding assays. Strictly avoid reducing agents including DTT, beta-mercaptoethanol, and TCEP — these agents reduce the disulfide bonds essential for Fc region homodimerisation and ActRIIB domain folding, destroying both ligand binding activity and the extended half-life properties of the intact fusion protein. Avoid repeated freeze-thaw cycles that cause irreversible aggregation — prepare single-use aliquots at the time of reconstitution and store at -80°C. For cell-based Smad2/3 inhibition assays, prepare ACE-031 working solutions in serum-free or low-serum media and add to cells simultaneously with or immediately before recombinant GDF-8 or activin A — pre-incubation of ACE-031 with the activating ligand before addition to cells is an effective experimental approach for confirming ligand-dependent inhibition. Monitor for protein aggregation by visual inspection and dynamic light scattering where available — aggregated ACE-031 shows reduced ligand binding capacity and potentially altered Fc receptor interactions that could confound biological activity measurements.
Every order of ACE-031 in Ireland includes:
✅ Batch-Specific Certificate of Analysis (CoA)
✅ HPLC Chromatogram
✅ Mass Spectrometry Confirmation
✅ Sterility & Endotoxin Testing Report
✅ Reconstitution Protocol — including Fc-fusion protein handling and carrier protein guidance
✅ Technical Research Support
Yes — we supply research-grade ACE-031 to researchers and institutions across Ireland with fast dispatch and full batch documentation. This compound is supplied strictly for laboratory research purposes only.
ACE-031 and anti-myostatin antibodies represent fundamentally different approaches to ActRIIB pathway inhibition that produce qualitatively and quantitatively distinct biological effects — making them complementary rather than equivalent research tools for studying different aspects of muscle mass regulation. Anti-myostatin antibodies bind and neutralise myostatin specifically — preventing GDF-8 from engaging ActRIIB while leaving activin A, GDF-11, and other ActRIIB ligands free to bind and activate the receptor. The result is selective relief of myostatin-mediated muscle growth inhibition while the inhibitory contributions of other ActRIIB ligands are maintained — producing meaningful but submaximal muscle hypertrophy that reflects the partial reduction in total ActRIIB inhibitory burden. ACE-031’s ActRIIB extracellular domain traps all ActRIIB-binding ligands simultaneously — including myostatin, activin A, GDF-11, and BMP-9/BMP-10 — producing complete relief of the total ActRIIB ligand burden and the profoundly greater muscle hypertrophy that results from removing all convergent inhibitory inputs simultaneously. For research purposes, the comparison between anti-myostatin antibody-treated and ACE-031-treated animals at matched experimental conditions provides a direct readout of the incremental contribution of non-myostatin ActRIIB ligands — primarily activin A — to the total muscle growth inhibitory signal, making this comparison one of the most scientifically informative experimental designs in ActRIIB ligand biology research.
The superior muscle hypertrophy produced by ACE-031 relative to myostatin-selective inhibitors reflects the multi-ligand nature of ActRIIB-mediated muscle mass regulation — a biological reality established through the comparative inhibition research enabled by ACE-031 as a research tool. Skeletal muscle cells are simultaneously exposed to multiple ActRIIB ligands circulating in the systemic and local tissue environment — myostatin being the most abundant and extensively characterised, but activin A making a quantitatively significant contribution to the total Smad2/3-activating signal in muscle, particularly in disease states including cancer cachexia and ageing where activin A levels are elevated. When myostatin is selectively neutralised, activin A and GDF-11 continue to bind ActRIIB and activate Smad2/3 signalling — maintaining a significant fraction of the total Smad2/3 atrophy programme despite complete myostatin inhibition and limiting the achievable muscle hypertrophy to the fraction of growth restraint attributable to myostatin alone. ACE-031 removes the entire ActRIIB ligand burden simultaneously — allowing full de-repression of Akt/mTOR anabolic signalling, complete suppression of MuRF1/atrogin-1 atrophy gene expression, and unrestricted satellite cell activation and myogenic programme progression — producing the maximal hypertrophic response accessible through this pathway. The biological magnitude of this difference — typically 1.5 to 2-fold greater muscle hypertrophy with pan-ActRIIB inhibition compared with myostatin-selective inhibition — has been the primary evidence establishing activin A as a physiologically important muscle mass regulator alongside myostatin.
The neutralisation of BMP-9 and BMP-10 by ACE-031’s ActRIIB extracellular domain represents a biologically significant off-target effect relative to ACE-031’s intended muscle regulatory ligand neutralisation — and the clinical consequences of this BMP neutralisation have made it an important research topic in its own right. BMP-9 and BMP-10 are critical regulators of vascular endothelial quiescence — signalling through the ALK1 receptor on endothelial cells to maintain the quiescent, non-angiogenic endothelial phenotype that characterises the mature stabilised vasculature. When BMP-9 and BMP-10 are neutralised by ACE-031’s extracellular domain — which binds these BMPs through its ActRIIB ligand-binding interface — endothelial cells lose the quiescence-maintaining ALK1 signal and can adopt an activated, angiogenic phenotype characterised by increased permeability and vascular remodelling. The clinical manifestation of this biology in ACE-031-treated subjects — telangiectasia and epistaxis reflecting abnormal vascular remodelling and fragility — provided direct evidence for the physiological importance of BMP-9/BMP-10 signalling in human vascular biology and established that broad ActRIIB ligand neutralisation strategies must account for this vascular BMP biology. For research purposes, ACE-031 provides a pharmacological tool for studying the vascular biology consequences of BMP-9 and BMP-10 neutralisation — characterising how loss of these vascular quiescence signals produces endothelial activation, vascular remodelling, and the pathological vascular phenotypes relevant to hereditary haemorrhagic telangiectasia biology in which ALK1 loss-of-function mutations produce similar vascular pathology.
ACE-031 belongs to a broader class of ActRIIB extracellular domain-Fc fusion proteins that have been developed with varying ActRIIB domain sequences, linker designs, Fc isotypes, and amino acid modifications aimed at optimising ligand binding selectivity, half-life, and vascular safety profiles relative to the original ACE-031 design. Luspatercept and sotatercept — later generation TGF-beta superfamily ligand traps developed by Acceleron Pharma — use modified ActRIIB-related extracellular domains with altered ligand binding selectivity that reduce BMP-9/BMP-10 neutralisation while maintaining activity against activin ligands, and have proceeded further in clinical development for anaemia and related indications. Research comparing ACE-031 with these modified ligand trap designs has contributed to understanding of the structure-activity relationships governing ActRIIB extracellular domain ligand selectivity — characterising which amino acid positions within the ActRIIB binding interface determine differential affinity for myostatin, activin A, GDF-11, and the vascular BMPs. For muscle biology research, ACE-031 remains the reference pan-ActRIIB ligand trap for studying the complete ActRIIB ligand ensemble and its collective contribution to muscle mass regulation — while the modified selectivity profiles of later generation ligand traps provide complementary research tools for dissecting the individual ligand contributions to the biological effects of pan-ActRIIB pathway inhibition.
Rigorous ACE-031 research design requires several critical controls for mechanistic interpretation. Vehicle controls matched to the ACE-031 reconstitution solvent — PBS with carrier protein at equivalent concentration — must be included in all cell-based and in vivo studies to control for non-specific protein and buffer effects. Myostatin-selective inhibitor parallel treatment groups — anti-myostatin antibody or myostatin propeptide at doses producing equivalent myostatin neutralisation — are essential for dissecting the myostatin-specific versus pan-ActRIIB components of ACE-031’s biological effects and should be included in all comparative ActRIIB ligand biology studies. Ligand specificity validation — confirming that observed ACE-031 effects are reversed by exogenous supplementation with recombinant GDF-8 or activin A at concentrations exceeding ACE-031’s ligand trapping capacity — provides mechanistic confirmation of ligand-dependent activity. For in vivo muscle hypertrophy studies, histological characterisation of fibre size, fibre number, satellite cell density, and fibre type composition alongside mass measurements provides complete cellular characterisation of the hypertrophic response. For vascular biology studies examining BMP-9/BMP-10 effects, endothelial cell activation markers, vascular permeability measurements, and histological vascular examination are important for characterising the vascular biology consequences of broad ActRIIB ligand neutralisation at the doses used.
ACE-031 has been examined across a range of pre-clinical disease models — with cancer cachexia, Duchenne muscular dystrophy, and sarcopenia representing the most extensively studied research contexts. Cancer cachexia models — including colon-26 carcinoma, Lewis lung carcinoma, and patient-derived tumour xenograft models in rodents — have been used to characterise ACE-031’s capacity to preserve muscle mass in the context of tumour-derived catabolic signals, with particular research focus on the role of tumour-derived activin A as a driver of cachexia muscle wasting that is specifically neutralised by ACE-031’s activin A trapping. Duchenne muscular dystrophy research using the mdx mouse model has characterised ACE-031’s muscle hypertrophic and regeneration-enhancing effects in dystrophin-deficient muscle — examining whether the muscle mass gains achieved through ActRIIB ligand neutralisation translate into functional improvement in the context of ongoing fibre necrosis. Ageing-associated sarcopenia models using aged rodents have examined whether elevated ActRIIB ligand signalling contributes to age-related muscle loss and whether ACE-031 treatment can restore muscle mass toward youthful levels in aged animals. Spinal muscular atrophy models have been examined — with ACE-031 used to study whether ActRIIB pathway inhibition can maintain muscle mass in the context of motor neuron loss and denervation atrophy.
≥99% purity is strongly recommended for ActRIIB ligand binding studies, Smad2/3 pathway inhibition research, muscle hypertrophy biology, disease model research, and all pre-clinical studies where ligand binding specificity, inhibitory potency characterisation, and mechanistic attribution are primary requirements. For ACE-031 as a recombinant Fc-fusion protein, purity assessment encompasses not only chemical identity but also the structural integrity of the ActRIIB extracellular domain fold — confirming that the protein is correctly folded and capable of ligand binding rather than comprising misfolded or aggregated material that could show altered ligand selectivity or reduced binding affinity. In ligand competition and inhibitor screening assays where ACE-031 serves as a reference pan-ActRIIB ligand trap, batch-to-batch consistency in ligand binding affinity is essential for reproducible IC50 and inhibition potency determinations. For in vivo muscle wasting disease models where the research question concerns the biological consequences of maximal ActRIIB ligand neutralisation, high purity and confirmed biological activity by ActRIIB ligand binding assay before in vivo use ensures that the administered protein produces the intended pharmacological effect. All ACE-031 Ireland stock is independently verified to ≥99% purity by HPLC and mass spectrometry with Fc-fusion protein identity and ActRIIB domain integrity confirmation.
ACE-031 is supplied exclusively for legitimate scientific research purposes conducted within licensed laboratory environments. This product is not intended for human consumption, self-administration, or any therapeutic application. It must be handled by qualified researchers in compliance with applicable Irish and EU regulations and institutional ethics guidelines. By purchasing, you confirm that this compound will be used solely for approved in vitro or pre-clinical research purposes.
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