AICAR | Buy Research-Grade AICAR in Europe | ≥99% Purity

AICAR (5-Aminoimidazole-4-carboxamide ribonucleotide; Acadesine) is a naturally occurring cell-permeable AMP analogue and potent AMPK activator, available to buy in Europe for laboratory research into AMPK pathway biology, cellular energy sensing, mitochondrial biogenesis, autophagy, glucose and lipid metabolism, cancer cell metabolism, and the comparative pharmacology of AMPK-activating compounds.

Laboratories and research institutions across the EU can order verified, research-grade AICAR with fast international dispatch to Europe, full batch documentation, and ≥99% purity confirmed by HPLC and Mass Spectrometry.

✅ ≥99% Purity — HPLC & Mass Spectrometry Verified

✅ Batch-Specific Certificate of Analysis (CoA)

✅ Sterile Lyophilised Powder | GMP Manufactured

✅ Fast Dispatch to EU & Europe | Tracked Shipping

What is AICAR?

AICAR (5-Aminoimidazole-4-carboxamide-1-β-D-ribofuranoside; Acadesine) is a naturally occurring nucleoside analogue and intermediate of the de novo purine biosynthesis pathway. Upon cellular uptake via adenosine transporters, AICAR is phosphorylated by adenosine kinase to its monophosphorylated form ZMP (AICAR monophosphate; 5-aminoimidazole-4-carboxamide ribonucleotide 5′-monophosphate) — the metabolically active species that accumulates intracellularly and mediates AICAR’s primary pharmacological effects. ZMP is a structural analogue of AMP and mimics AMP’s allosteric activation of AMP-activated protein kinase (AMPK) — binding the γ-subunit regulatory sites of AMPK and inducing conformational changes that activate the kinase, suppress its dephosphorylation by protein phosphatases, and drive the downstream signalling programme associated with cellular energy deficit.

AMPK is the master sensor and regulator of cellular energy homeostasis — a heterotrimeric serine/threonine kinase complex composed of a catalytic α-subunit (α1/α2) and regulatory β- and γ-subunits that senses the cellular AMP:ATP and ADP:ATP ratios as indicators of energy status. Under conditions of energy deficit — exercise, nutrient deprivation, hypoxia, or ischaemia — rising AMP and ADP levels allosterically activate AMPK through γ-subunit nucleotide binding, and upstream kinases LKB1 and CaMKKβ phosphorylate the critical α-subunit Thr172 residue to produce full kinase activation. Activated AMPK phosphorylates a broad substrate network that collectively restores energy balance: inhibiting ATP-consuming anabolic processes (fatty acid synthesis through ACC1/2 phosphorylation, protein synthesis through mTORC1 inhibition via raptor and TSC2 phosphorylation, glycogen synthesis through GS phosphorylation) while activating ATP-generating catabolic processes (fatty acid oxidation through ACC2 inactivation and CPT1 activation, glycolysis through PFKFB3 phosphorylation, mitochondrial biogenesis through PGC-1α activation). AICAR/ZMP mimics this energy deficit signal pharmacologically — activating AMPK without actually depleting ATP — providing a tool to study AMPK pathway biology in cells under energy-replete conditions where endogenous AMPK activation would otherwise be minimal.

The distinction between AICAR’s primary mechanism (ZMP-mediated AMPK activation) and its secondary effects (direct inhibition of the fructose-1,6-bisphosphatase enzyme involved in gluconeogenesis; interference with AMP deaminase activity) is important for mechanistic research interpretation. ZMP’s structural similarity to AMP means it can engage multiple AMP-sensitive enzymes beyond AMPK — making compound C (dorsomorphin) AMPK inhibitor controls and genetic AMPK knockdown/knockout systems essential companions to AICAR in mechanistic studies. This complexity has driven development of more AMPK-selective activators (A-769662, MK-8722, PF-06409577) — with AICAR remaining the most widely used pharmacological AMPK activation tool due to its cell permeability, well-characterised biology, and extensive comparative literature.

What Does AICAR Do in Research?

In laboratory settings, AICAR is studied across AMPK pathway biology, metabolic regulation, mitochondrial function, autophagy, cancer metabolism, cardioprotection, and skeletal muscle biology. EU and European researchers working with AICAR typically focus on:

AMPK pathway activation and energy sensing biology — AICAR is the most widely used and extensively characterised pharmacological AMPK activator — providing a cell-permeable tool for activating AMPK through ZMP-mediated γ-subunit engagement in the same allosteric mechanism as endogenous AMP. Studies use AICAR to activate AMPK in diverse cell types under energy-replete conditions — characterising α-subunit Thr172 phosphorylation dynamics, the downstream substrate phosphorylation cascade, and the broad metabolic and transcriptional consequences of AMPK activation in cell biology research. AICAR is used alongside genetic AMPK activation (constitutively active AMPK mutants) and pharmacological AMPK inhibition (compound C) to establish the AMPK-dependence of observed cellular responses and map the AMPK substrate network.

Mitochondrial biogenesis and PGC-1α research — AMPK activation by AICAR drives phosphorylation and deacetylation of PGC-1α — the master transcriptional co-activator of mitochondrial biogenesis — through direct AMPK-mediated PGC-1α phosphorylation at Thr177 and Ser538 and indirect AMPK-driven SIRT1 activation through NAD⁺ elevation. PGC-1α activation drives expression of nuclear-encoded mitochondrial genes — including those encoding oxidative phosphorylation subunits, TCA cycle enzymes, and mitochondrial import machinery — producing increased mitochondrial mass, enhanced oxidative capacity, and improved cellular respiratory function. Studies use AICAR to examine AMPK-driven mitochondrial biogenesis — characterising PGC-1α target gene induction, mitochondrial DNA copy number, oxygen consumption rate increases, and the SIRT1-dependent and SIRT1-independent components of AMPK/PGC-1α pathway activation.

Autophagy and mitophagy research — AMPK activates autophagy through two convergent mechanisms: direct phosphorylation and activation of ULK1 (the mammalian autophagy initiating kinase, at Ser317 and Ser555) and suppression of mTORC1 (the primary ULK1 inhibitory kinase) through raptor phosphorylation and TSC2 activation. The resulting ULK1 disinhibition and direct activation drives phagophore nucleation, autophagosome formation, and autophagic flux — including selective mitophagy of damaged mitochondria. Studies use AICAR to examine AMPK-dependent autophagy induction — characterising ULK1 phosphorylation, LC3-II accumulation, p62/SQSTM1 degradation, autophagosome formation, and the AMPK versus mTORC1 signalling balance that determines autophagic activity under different metabolic conditions.

Glucose metabolism and insulin signalling research — AMPK activation by AICAR increases glucose uptake in skeletal muscle through GLUT4 translocation to the plasma membrane via an insulin-independent, PI3K-independent mechanism — a finding with significant implications for metabolic disease research. Studies use AICAR to examine AMPK-dependent glucose transport — characterising GLUT4 vesicle trafficking, Rab GTPase regulation, and the AMPK substrate network mediating insulin-independent glucose uptake — and to probe the relationship between AMPK activation, insulin signalling, and the additive versus synergistic effects of combined AMPK and insulin receptor pathway stimulation on glucose disposal in muscle cell systems.

Fatty acid oxidation and lipid metabolism research — AMPK phosphorylates and inhibits acetyl-CoA carboxylase 1 and 2 (ACC1/ACC2) — the rate-limiting enzymes of fatty acid synthesis and the primary regulators of malonyl-CoA levels. Malonyl-CoA inhibits carnitine palmitoyltransferase 1 (CPT1) — the rate-limiting enzyme of long-chain fatty acid entry into mitochondria for β-oxidation. AICAR-driven AMPK activation therefore simultaneously suppresses fatty acid synthesis (ACC1 phosphorylation) and relieves CPT1 inhibition (ACC2 phosphorylation, malonyl-CoA reduction) — producing a coordinated shift from lipid storage toward lipid oxidation. Studies use AICAR to examine ACC phosphorylation kinetics, malonyl-CoA dynamics, CPT1 activity, fatty acid oxidation rates, and the transcriptional regulation of lipid metabolism genes through AMPK-driven SREBP1c and ChREBP suppression.

mTORC1 pathway and protein synthesis research — AMPK suppresses mTORC1 activity through two parallel mechanisms: direct phosphorylation of the mTORC1 scaffold protein raptor (at Ser722/792), which inhibits mTORC1 complex assembly and activity; and phosphorylation of TSC2 (at Ser1387), which activates the TSC1/TSC2 Rheb-GAP complex and suppresses Rheb-GTP-dependent mTORC1 activation. The resulting mTORC1 inhibition reduces S6K1 and 4E-BP1 phosphorylation, suppressing cap-dependent mRNA translation and protein synthesis — conserving ATP under energy-limiting conditions. Studies use AICAR to probe AMPK-mediated mTORC1 suppression — characterising raptor and TSC2 phosphorylation, the kinetics of S6K1 and 4E-BP1 dephosphorylation, and the downstream translational consequences of AMPK-driven mTORC1 inhibition in cells under various nutrient and growth factor conditions.

Skeletal muscle metabolism and exercise mimicry research — AICAR-driven AMPK activation in skeletal muscle produces metabolic adaptations that parallel those of endurance exercise — including GLUT4 upregulation, PGC-1α-driven mitochondrial biogenesis, increased fatty acid oxidation capacity, and fibre-type composition shifts toward oxidative fibre phenotypes. Studies in rodent models have established that chronic AICAR administration produces exercise-like skeletal muscle metabolic adaptations in sedentary animals — providing a pharmacological tool for studying exercise-induced metabolic adaptation mechanisms and separating AMPK-dependent from AMPK-independent components of the exercise adaptation programme. These exercise mimicry studies have established AICAR as a reference compound for the pharmacology of skeletal muscle metabolic plasticity.

Cardioprotection and ischaemic preconditioning research — AMPK activation in cardiac muscle during ischaemia is a protective adaptive response — increasing glucose uptake, fatty acid oxidation, and autophagy while suppressing energy-consuming anabolic processes. AICAR has been extensively studied in cardiac ischaemia-reperfusion and ischaemic preconditioning models — with pre-clinical studies documenting reduced infarct size, preserved mitochondrial function, and improved cardiac function recovery following AICAR treatment through AMPK-dependent cardioprotective mechanisms. These cardioprotection studies have established AICAR as the reference pharmacological AMPK activation tool in cardiac ischaemia research.

Cancer cell metabolism and AMPK tumour suppression research — AMPK acts as a metabolic tumour suppressor — its activation by the upstream kinase LKB1 (a tumour suppressor frequently mutated in Peutz-Jeghers syndrome and lung cancer) driving mTORC1 suppression, limiting anabolic biosynthesis, and imposing the metabolic checkpoint that prevents cancer cell proliferation under energetic stress. Studies use AICAR to examine AMPK-dependent cancer cell growth suppression — characterising mTORC1 inhibition, cell cycle arrest, reduced nucleotide and lipid biosynthesis, and the LKB1-dependent versus LKB1-independent AMPK activation mechanisms in cancer cell lines. AICAR is also used to study the Warburg effect — aerobic glycolysis in cancer cells — and the metabolic vulnerabilities created by cancer-specific AMPK pathway dysregulation.

Hepatic glucose production and gluconeogenesis research — AMPK activation in hepatocytes suppresses gluconeogenic gene expression — including PEPCK and G6Pase — through TORC2/CREB pathway inhibition and FOXO1 regulation, reducing hepatic glucose output. AICAR additionally inhibits fructose-1,6-bisphosphatase directly as a ZMP-dependent AMPK-independent mechanism — providing dual suppression of gluconeogenesis. Studies use AICAR in hepatocyte preparations and liver-specific AMPK models to examine AMPK-dependent and ZMP-dependent components of gluconeogenesis suppression — characterising the relative contributions of transcriptional regulation and allosteric enzyme inhibition to AICAR’s anti-gluconeogenic effects and their relevance to insulin-resistant hepatic glucose overproduction in type 2 diabetes models.

Inflammation and NF-κB pathway research — AMPK activation suppresses inflammatory signalling through multiple mechanisms — direct phosphorylation and activation of IKKβ-inhibiting phosphatases, suppression of NF-κB-driven pro-inflammatory gene expression, and mTORC1 inhibition reducing the translational upregulation of cytokine production. AICAR has been studied in macrophage, endothelial, and epithelial inflammatory systems — with findings documenting suppressed LPS-stimulated TNF-α, IL-1β, and IL-6 production and reduced NF-κB nuclear translocation. Studies use AICAR to characterise AMPK-dependent anti-inflammatory signalling — establishing the mechanistic connections between cellular energy status, AMPK activation, and inflammation resolution in metabolic and immune cell systems.

AMPK isoform selectivity and subunit composition research — AMPK exists as multiple heterotrimeric combinations of α1/α2 catalytic subunits, β1/β2 scaffold subunits, and γ1/γ2/γ3 regulatory subunits — with different isoform combinations exhibiting distinct tissue distributions, subcellular localisations, and regulatory properties. AICAR activates all AMPK isoforms through the shared γ-subunit ZMP binding mechanism — making it useful in comparative isoform studies where pan-AMPK activation is required, and in combination with isoform-selective genetic approaches to dissect the biology of specific AMPK heterotrimeric combinations.

All research applications are for in vitro and pre-clinical use only.

What Do Studies Say About AICAR?

AICAR has one of the most extensive research literatures of any metabolic research compound — spanning decades of biochemical characterisation of purine metabolism, foundational AMPK biology, metabolic disease pre-clinical research, and cancer metabolism studies.

AMPK activation mechanism characterisation: Foundational studies by Corton, Hardie, Carling, and colleagues established ZMP as an AMP analogue that activates AMPK by binding γ-subunit nucleotide-binding sites — producing the same allosteric activation and Thr172 dephosphorylation protection as physiological AMP. These AICAR/ZMP mechanistic studies were instrumental in establishing the γ-subunit nucleotide-sensing mechanism of AMPK regulation and validated AICAR as a pharmacological tool for AMP-mimetic AMPK activation. The identification that AICAR’s active form is ZMP — requiring intracellular phosphorylation by adenosine kinase — established the importance of adenosine kinase activity in determining cellular AICAR sensitivity.

Skeletal muscle glucose transport and exercise adaptation: Studies by Hayashi, Hardie, Goodyear, and colleagues documented AICAR-stimulated glucose uptake in isolated skeletal muscle through an insulin-independent GLUT4 translocation mechanism — establishing that AMPK activation is sufficient to drive muscle glucose uptake without insulin receptor engagement. The subsequent demonstration that chronic AICAR administration in rodents produces exercise-like metabolic adaptations — including mitochondrial biogenesis, increased oxidative enzyme expression, and enhanced endurance capacity — established AICAR as the reference exercise mimicry compound and provided the experimental foundation for the concept of pharmacological exercise adaptation.

PGC-1α and mitochondrial biogenesis: Studies characterising AICAR-driven PGC-1α activation documented AMPK-dependent PGC-1α phosphorylation, SIRT1-mediated deacetylation, and downstream mitochondrial gene induction — establishing the AMPK/PGC-1α/mitochondrial biogenesis axis as a central adaptive response to energy deficit signals. These mitochondrial biogenesis studies positioned AICAR as the key pharmacological tool for activating the exercise-responsive transcriptional programme governing mitochondrial content and oxidative capacity.

Cardioprotection and ischaemia-reperfusion studies: Extensive pre-clinical studies in rodent and large animal cardiac ischaemia-reperfusion models documented AICAR-mediated cardioprotection — reduced infarct size, preserved ATP levels during ischaemia, reduced cardiomyocyte apoptosis, and improved post-ischaemic cardiac function recovery. These cardiac protection studies established AICAR as the reference AMPK activator in cardiac ischaemia research and led to clinical investigation of acadesine (AICAR) as a perioperative cardioprotective agent in cardiac surgery — providing a translational research context for the pre-clinical AMPK cardioprotection literature.

AMPK tumour suppression and LKB1 biology: Studies characterising AICAR in cancer cell systems — particularly in LKB1-expressing versus LKB1-deficient cancer cell lines — established the LKB1/AMPK/mTORC1 tumour suppression pathway as a central growth-suppressive mechanism in cancer biology. AICAR-driven AMPK activation in LKB1-competent cancer cells produced mTORC1 suppression, cell cycle arrest, and reduced proliferation — while LKB1-deficient cancer cells exhibited reduced AMPK activation in response to AICAR and maintained mTORC1 activity. These studies established AICAR as a tool for probing LKB1/AMPK pathway integrity in cancer cell biology and characterising the metabolic checkpoint function of the LKB1/AMPK axis.

Autophagy pathway characterisation: Studies documenting AICAR-driven autophagy induction characterised the AMPK/ULK1 activation mechanism — establishing direct AMPK phosphorylation of ULK1 as a distinct autophagy-initiating pathway parallel to mTORC1-dependent ULK1 regulation. These AICAR autophagy studies contributed foundational mechanistic data to the autophagy field, establishing the dual AMPK-dependent (ULK1 activation) and AMPK-indirect (mTORC1 suppression/ULK1 disinhibition) mechanisms of energy deficit-driven autophagy induction.

AICAR limitations and selectivity considerations: Studies examining AICAR’s pharmacological profile beyond AMPK documented ZMP’s interaction with multiple AMP-sensitive enzymes — including fructose-1,6-bisphosphatase inhibition, AMP deaminase inhibition, and direct effects on adenylate cyclase — establishing that not all AICAR-driven cellular changes are AMPK-mediated. These selectivity studies motivated the development of more AMPK-selective activators (A-769662 targeting the β-subunit allosteric drug-binding site; MK-8722 and PF-06409577 as β1-selective allosteric activators) and established the importance of compound C inhibitor controls and genetic AMPK knockdown approaches in mechanistic AICAR research.

AICAR vs Related AMPK Pathway Research Compounds

Compound	Class	AMPK Activation Mechanism	AMPK Selectivity	Primary Research Application	Key Research Distinction
AICAR (Acadesine)	Cell-permeable AMP nucleoside analogue	ZMP-mediated γ-subunit allosteric activation (AMP-mimetic)	Moderate — ZMP engages multiple AMP-sensitive enzymes	Reference AMPK activator; metabolic research; exercise mimicry; cardioprotection	Most widely used AMPK activator; broadest comparative literature; multiple AMP-sensitive enzyme effects
A-769662	Synthetic thienopyridone	β-subunit allosteric drug-binding site (non-AMP-mimetic)	High — β-subunit site not shared with other AMP enzymes	AMPK-selective activation without AMP-mimetic off-targets	More AMPK-selective than AICAR; β1-subunit preferring; does not activate AMP-sensitive enzymes
MK-8722	Small molecule allosteric activator	β-subunit allosteric site	High — pan-β (β1/β2)	Systemic AMPK activation; in vivo metabolic studies	Pan-β isoform activator; more potent than A-769662; in vivo pharmacokinetics studied
Compound C (Dorsomorphin)	Small molecule ATP-competitive inhibitor	AMPK inhibition — ATP-competitive at α-subunit kinase domain	Moderate — inhibits other kinases (BMP receptor kinases)	AMPK inhibitor control for AICAR studies	Reference AMPK inhibitor; used to confirm AMPK-dependence of AICAR responses
Metformin	Biguanide — complex I inhibitor	Indirect AMPK activation via mitochondrial complex I inhibition → AMP:ATP ratio rise	Indirect — acts upstream via energy deficit	Type 2 diabetes; hepatic glucose production; clinical AMPK activator reference	Clinically used indirect AMPK activator; complex I mechanism; hepatic selectivity
2-Deoxyglucose (2-DG)	Glucose analogue — glycolysis inhibitor	Indirect AMPK activation via ATP depletion	Indirect — broad metabolic disruption	Glycolysis inhibition; energy stress model	Metabolic stress control — ATP-depleting AMPK activator; direct energy depletion vs AICAR ZMP-mimicry
Rapamycin	mTORC1 allosteric inhibitor (FKBP12-dependent)	No AMPK activation — acts downstream	mTORC1-selective	mTORC1 inhibition reference; AMPK/mTORC1 pathway dissection	Downstream AMPK target inhibitor; used alongside AICAR to confirm mTORC1 as AMPK effector

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Buying AICAR in Europe — What’s Included

Every order of AICAR dispatched to EU and European research institutions includes:

• Batch-Specific Certificate of Analysis (CoA)
• HPLC Chromatogram
• Mass Spectrometry Confirmation
• Sterility and Endotoxin Testing Reports
• Reconstitution Protocol
• Technical Research Support

Frequently Asked Questions — AICAR EU

Can I Buy AICAR in the EU and Europe?

Yes. We supply research-grade AICAR with fast tracked dispatch to all EU member states and wider European destinations. All orders include full batch documentation. AICAR is supplied strictly for laboratory research use only.

What is the Difference Between AICAR and ZMP — Which is the Active Species?

AICAR (the free nucleoside, 5-aminoimidazole-4-carboxamide ribonucleoside) is the cell-permeable prodrug form — taken up by cells via adenosine nucleoside transporters. Once inside the cell, AICAR is phosphorylated by adenosine kinase at the 5′ ribose position to generate ZMP (AICAR monophosphate; 5-aminoimidazole-4-carboxamide ribonucleotide 5′-monophosphate) — the metabolically active charged species that accumulates intracellularly and mediates AICAR’s pharmacological effects. ZMP is structurally analogous to AMP — carrying a negatively charged monophosphate group that prevents membrane permeation — explaining why ZMP itself cannot be directly added to cells to replicate AICAR’s effects in intact cell systems. The distinction is important for mechanistic research: cell-free biochemical assays examining AMPK allosteric activation use ZMP directly, while intact cell studies use AICAR as the membrane-permeable prodrug that generates ZMP intracellularly following adenosine kinase-mediated phosphorylation.

What is AMPK and Why is it Considered the Master Energy Sensor?

AMP-activated protein kinase (AMPK) is a heterotrimeric serine/threonine kinase comprising a catalytic α-subunit (α1 or α2) and regulatory β- (β1 or β2) and γ- (γ1, γ2, or γ3) subunits. AMPK earns the designation of master energy sensor through its unique biochemical design: the γ-subunit contains four cystathionine β-synthase (CBS) domain pairs forming two Bateman domains that bind AMP, ADP, and ATP in a mutually competitive manner. When the cellular AMP:ATP ratio rises — indicating energy deficit from increased ATP consumption or decreased ATP production — AMP outcompetes ATP for γ-subunit binding, producing three convergent activating effects: allosteric activation of the already-phosphorylated kinase, protection of the critical α-subunit Thr172 residue from dephosphorylation by PP2A/PP2C phosphatases, and promotion of upstream kinase (LKB1, CaMKKβ)-mediated Thr172 phosphorylation. This three-mechanism amplification of the AMP signal makes AMPK exquisitely sensitive to energy status changes — with ZMP’s AMP mimicry engaging this same γ-subunit sensing mechanism to pharmacologically activate AMPK under energy-replete conditions.

How Does AICAR Relate to Metformin as an AMPK Research Tool?

Both AICAR and metformin activate AMPK but through fundamentally different mechanisms — making them complementary rather than interchangeable research tools. AICAR acts directly as an AMP-mimetic prodrug — generating ZMP intracellularly to allosterically activate AMPK without depleting ATP. Metformin inhibits mitochondrial respiratory chain complex I — reducing oxidative phosphorylation-driven ATP production, increasing the AMP:ATP ratio, and activating AMPK indirectly through the physiological energy deficit pathway. For mechanistic research, this distinction is critical: AICAR-driven AMPK activation occurs at normal ATP levels and with minimal energy stress, making it suitable for studying AMPK pathway biology in isolation. Metformin-driven AMPK activation is accompanied by genuine ATP depletion and mitochondrial effects — complicating attribution of observed effects to AMPK specifically versus energy depletion broadly. AICAR is therefore preferred when clean, ATP-depletion-independent AMPK activation is required for mechanistic research; metformin is used when clinically relevant indirect AMPK activation or complex I biology is the research focus.

What Are the Limitations of AICAR as an AMPK Research Tool?

AICAR’s primary research limitation is ZMP’s structural similarity to AMP, which means ZMP engages multiple AMP-sensitive enzymes beyond AMPK. The best-characterised off-target effects include: direct inhibition of fructose-1,6-bisphosphatase (FBPase) — the key gluconeogenic enzyme — producing ZMP/AMPK-independent suppression of hepatic glucose production; inhibition of AMP deaminase — altering adenylate metabolism; and potential effects on adenylate cyclase and other AMP-regulated enzymes. These off-target effects require that AMPK-dependence of AICAR responses be confirmed using compound C (AMPK inhibitor) controls, genetic AMPK knockdown or knockout approaches, or comparison with structurally distinct AMPK activators (A-769662) that act through the β-subunit allosteric site rather than the γ-subunit AMP-mimetic mechanism. AICAR also requires functional adenosine kinase activity for ZMP generation — making it inactive in adenosine kinase-deficient cell lines and motivating direct ZMP use in cell-free biochemical assays.

Why is AICAR Called an Exercise Mimetic?

The exercise mimicry designation for AICAR arises from studies demonstrating that chronic AICAR administration in rodents produces skeletal muscle metabolic adaptations that parallel those of endurance exercise training — including increased mitochondrial biogenesis through PGC-1α activation, upregulated oxidative enzyme expression, increased GLUT4 density, enhanced fatty acid oxidation capacity, and partial shifts toward oxidative muscle fibre phenotypes — without the mechanical activity of exercise itself. These AICAR-driven adaptations are AMPK-dependent, mirroring the role of AMPK as a key mediator of exercise-induced skeletal muscle metabolic adaptation. The exercise mimicry concept positions AICAR as a research tool for studying the AMPK-dependent component of the exercise adaptation programme — dissecting which adaptations require AMPK activation alone (reproduced by AICAR) from those requiring additional exercise-specific signals such as mechanical loading, calcium transients, reactive oxygen species, and other exercise-associated stimuli (not reproduced by AICAR).

How Do I Reconstitute AICAR for Laboratory Use?

Reconstitute with sterile water or PBS by adding solvent slowly down the vial wall and swirling gently. AICAR is a nucleoside with excellent water solubility — dissolving readily at concentrations up to 100 mM in aqueous buffers without organic co-solvents. Prepare working stock solutions at the required concentration (typical cell treatment concentrations range from 0.5–2 mM for most cell systems), aliquot into single-use volumes, and store at -20°C. AICAR is stable in solution at -20°C but should not be subjected to repeated freeze-thaw cycles. For cell treatment experiments, dilute to working concentration in pre-warmed cell culture medium immediately before use. Verify that the cell system expresses functional adenosine kinase for efficient ZMP generation — in adenosine kinase-deficient systems, direct ZMP addition to cell lysates or cell-free assay systems is required to achieve AMPK activation.

How Quickly is AICAR Delivered to Europe?

Delivery to EU and European destinations typically takes 3–7 working days via tracked international courier with packaging maintaining compound stability throughout transit.

Product Specifications

Parameter	Detail
Compound	AICAR (Acadesine; 5-Aminoimidazole-4-carboxamide-1-β-D-ribofuranoside)
Molecular Formula	C₉H₁₄N₄O₅
Molecular Weight	258.23 g/mol
Class	Cell-permeable AMP nucleoside analogue — AMPK activator prodrug
Active Intracellular Form	ZMP (AICAR monophosphate) — generated by adenosine kinase phosphorylation
Primary Mechanism	ZMP-mediated allosteric AMPK activation — γ-subunit AMP-mimetic binding
AMPK Activation	All AMPK heterotrimeric isoforms — pan-AMPK via γ-subunit ZMP binding
Secondary Mechanisms	FBPase inhibition (gluconeogenesis suppression); AMP deaminase inhibition
Key Downstream Targets	PGC-1α/mitochondrial biogenesis; ACC1/2 (lipid metabolism); mTORC1/raptor/TSC2; ULK1 (autophagy); GLUT4/glucose transport; NF-κB (anti-inflammatory)
Endogenous Context	Purine de novo biosynthesis pathway intermediate
Primary Research Interest	AMPK pathway biology, mitochondrial biogenesis, autophagy, skeletal muscle metabolism, cardioprotection, cancer metabolism, hepatic glucose production, exercise mimicry
Purity	≥99%
Verification	HPLC & Mass Spectrometry
Form	Sterile Lyophilised Powder
Solubility	Highly water-soluble — sterile water or PBS; no organic co-solvent required
Storage	-20°C, protected from light and moisture; avoid repeated freeze-thaw
Intended Use	Research use only

Research Disclaimer

AICAR (Acadesine) is supplied exclusively for legitimate scientific research conducted within licensed laboratory environments. This product is not approved for human consumption, self-administration, or any therapeutic, clinical, or veterinary application. It must be handled solely by qualified researchers in compliance with applicable EU regulations, national legislation, and institutional ethics guidelines. By purchasing, you confirm this compound will be used exclusively for approved in vitro or pre-clinical research purposes.