Aicar Peptide | Aicar 50mg

Aicar Peptide Information

Aicar Peptide Overview

AICAR (50mg) research peptide is a high-quality laboratory reagent for scientific evaluation. In biochemical and physiological research, AICAR (5-Aminoimidazole-4-carboxamide ribonucleotide) is studied extensively for its role as an analog of adenosine monophosphate (AMP).

Researchers can investigate the effects of metabolic stress by mimicking AMP in cellular model without depleting ATP reserves. This product has been synthesized using strict quality control standards, ensuring the molecular stability required for reproducible high-throughput screens and experimental models.

Important Note: This product is a synthesized chemical reagent that has been manufactured exclusively for use in research. This product is not for use in diagnostic, therapeutic or human applications.

Aicar Features

• Research-Grade Formulation: Synthesized at a verified purity level exceeding 98% to ensure experimental consistency and minimize confounding variables.
• Lyophilized Peptide Format: Delivered as a stable, freeze-dried powder to maximize shelf-life integrity during transit and long-term storage.
• AMPK Signaling Applications: An established laboratory tool for the chemical activation of the AMP-activated protein kinase pathway in vitro.
• Strict Storage Optimization: Formulated to withstand standard laboratory storage protocols, maintaining stability under controlled thermal conditions.
• Compliant Research Designation: Packaged and distributed solely for analytical, veterinary, and laboratory research methodologies.

What is AICAR Peptide?

AICAR Peptide is the synthetic laboratory form of 5-Aminoimidazole-4-carboxamide ribonucleotide, a naturally occurring intermediary matrix within purine biosynthesis. It is often grouped with metabolic regulators in the scientific literature due to its cell permeable properties and direct interaction with cellular sensors.

When introduced to an experimental cellular model, AICAR is rapidly phosphorylated by adenosine kinase into its active form: ZMP (5-aminoimidazole-4-carboxamide ribonucleotide). ZMP is an intracellular analog to adenosine Monophosphate (AMP).

The AMPK-Related Research Overview

The enzyme AMP-activated Protein Kinase (AMPK), is the primary focus of AICAR research. Under normal physiological circumstances, a shift of ATP/AMP ratio signals cellular energy depletion. AMPK then activates catabolic pathways to increase energy generation and decrease anabolic pathway to conserve energy.

ZMP mimics AMP structurally, so it binds to the subunit $alpha$ of the AMPK homotrimer. This binding induces a change in conformation that encourages phosphorylation of upstream kinases and activates the AMPK cascade artificially. This biochemical mechanism allows researchers to isolate and observe the cellular adaptations under controlled laboratory conditions to simulated energy-deprivation.

Why Researchers Study AICAR

The ability to control cell signaling pathways in life sciences research is essential to mapping complex biochemical networks. Researchers use AICAR to trigger cellular stress models in a safe, non-lethal way without actually causing hypoxia or nutritional starvation.

1. Cellular Energy Regulation Research

Investigators use AICAR to evaluate the adaptation of cells to metabolic changes. This includes:

Transcription Factor Activation (e.g. PGC-1$alpha$).

Mitochondrial structure remodeling and biogenesis.

Glucose translocation (such GLUT4) occurs within the cellular membranes.

The modulation fatty acid oxidation routes.

2. Signaling upstream and downstream

By activating AMPK scientists can study cross-talks between energy sensing, and other fundamental biological systems. It is important to note that this is relevant for oncology models where researchers are assessing how the AMPK pathway modulates mTOR, a downstream pathway which regulates cell growth.

3. Standardize Workflows

The stability of AICAR 50mgvials allows highly standardized workflows. Since the lyophilized aqueous powder dissolves easily, it can be integrated into pipelines that prepare high-throughput assays, Western Blotting controls, or quantitative PCR.

Store and Handle Your Products Properly

It is important to comply with AICAR Peptide Storage protocol in order to prevent degradation, maintain peptide stability and ensure the validity of experimental results.

Initial Delivery and storage

The lyophilized vial must be checked for structural integrity upon receipt. The un-reconstituted Peptide must be kept in a laboratory freezer for long-term storage.

Short-Term storage (less than 3 months). Keep at 4℃ in a standard lab refrigerator.

Long Term Storage (Up To 24 Months): Maintain -20℃ or lower to avoid temperature fluctuations in a manual-defrost refrigerator.

Environmental Protection

The lyophilized product is sensitive to humidity and UV degradation. Vials must be stored in a dry environment, away from direct sunlight. Avoid repeated freeze-thaw cycles as they can cause peptide bond breakdown and reduce the potency of compounds.

Reconstitution Best Practices

Allow the vials to reach room temperature prior to opening them to avoid condensation.

• Use sterile Bacteriostatic Water or sterile Normal Saline to reconstitute, depending on the experimental matrix.
• Gently swirl the vial in order to promote dissolution. Do NOT shake or agitate the vial. Mechanical shear forces may denature synthetic peptide chain.
• To preserve remaining stock, it is recommended that you aliquote the solution and freeze them at -20℃ immediately after reconstitution.

FAQs

What is AICAR Peptide?

AICAR, a cell-permeable ribonucleoside synthesized from adenosine monphosphate (AMP), is a substitute for AMP. It is primarily utilized in laboratory settings to activate AMPK to study metabolic pathways, cellular energy regulation and AMPK.

What is the best way to store AICAR Peptide?

Aliquots of the reconstituted liquid should be frozen in order to avoid rapid degradation.

What is a lyophilized Peptide?

The term lyophilized is used in the freezing-drying of peptides under high vacuum. The liquid is converted into powder form, which increases shelf-life and protects molecular structure during shipping.

AICAR is intended to be used for research?

Yes. The product has been classified as Research use AICAR. This product is exclusively designed for use in laboratory tests, chemical assessments, and workflows that involve animal models. The product is not intended for human consumption or use in diagnostics.

What’s the difference between AICAR peptides and those used in research?

AICAR is an intracellular metabolic intermediary, unlike structural and hormonal research peptides which interact with receptors at the surface of cells. The AICAR directly targets the intracellular energy sensor by simulating a low energy state (high levels of AMP).

Can this product be used in cell culture assays?

AICAR high purity is used frequently in cell culture to activate metabolic pathways. Scientists must use established literature to determine the precise molar dose required for specific cell lines.

How pure is AICAR’s 50mg vial of AICAR?

Each batch of AICAR Research Peptide is tested via High Performance Liquid Chromatography and Mass Spectrometry to ensure that it meets or exceeds a 98% purity standard.

How should AICAR be dissolved?

AICAR lyophilized is usually dissolved in a sterile water solution, PBS, or sterile water bacteriostatic.

Scientific References

1. Corton, J. M., Gillespie, J. E., Hawley, S. A., & Hardie, D. G. (1995). 5-Aminoimidazole-4-carboxamide ribonucleoside: a specific method for activating AMP-activated protein kinase in intact cells? European Journal of Biochemistry, 229(2), 558–565.
2. Merrill, G. F., Kurth, E. J., Hardie, D. G., & Winder, W. W. (1997). AICA riboside increases AMP-activated protein kinase, fatty acid oxidation, and glucose uptake in rat muscle. American Journal of Physiology-Endocrinology and Metabolism, 273(6), E1107–E1112.
3. Hardie, D. G., & Carling, D. (1997). The AMP-activated protein kinase—fuel gauge of the mammalian cell. European Journal of Biochemistry, 246(2), 259–273.