AMARA peptide

Product Name: AMARA peptide

Sequence One Letter Code: AMARAASAAALARRR

Sequence Three Letter Code: H-Ala-Met-Ala-Arg-Ala-Ala-Ser-Ala-Ala-Ala-Leu-Ala-Arg-Arg-Arg-OH

Chemical Formula:C62H115N27O17S1

Molecular Weight: 1542.9

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: peptide substrate

Conjugation: Unconjugated

Code Nacres: NA.26

Application: AMARA peptide is a minimal consensus substrate commonly used to study AMP-activated protein kinase (AMPK) and related serine/threonine kinases. It contains a defined phosphorylation motif that is efficiently recognized and phosphorylated by AMPK, making it suitable for quantitative in vitro kinase assays. The peptide enables accurate measurement of kinase activity, enzyme kinetics, and substrate specificity. It is widely applied in screening assays for kinase modulators and in mechanistic studies of AMPK-regulated signaling pathways. AMARA peptide supports research in metabolic regulation, energy sensing, and signal transduction processes linked to cellular stress responses and metabolic disease.

Current Research: AMARA peptide is a synthetic minimal consensus substrate widely used for biochemical characterization of AMP-activated protein kinase (AMPK) and related basophilic serine/threonine kinases. The canonical AMARA sequence (AMARAASAAALARRR) contains a defined phosphorylation motif centered on a serine residue that conforms to the preferred AMPK recognition pattern, including basic residues at the −3 and −4 positions relative to the phosphorylation site. This optimized motif ensures efficient and reproducible phosphorylation in vitro. AMPK is a heterotrimeric kinase complex that functions as a central cellular energy sensor. It becomes activated under conditions of energetic stress—such as increased AMP/ATP or ADP/ATP ratios—and phosphorylates downstream substrates to restore energy balance by promoting catabolic pathways and inhibiting anabolic processes. Because endogenous AMPK substrates can be structurally complex and variably regulated, the AMARA peptide provides a simplified and well-defined model substrate for direct assessment of catalytic activity. In in vitro kinase assays, AMARA peptide is commonly used in combination with radiolabeled ATP (e.g., [γ-³²P]ATP), fluorescence-based phosphate detection systems, or mass spectrometry–based quantification. Its minimal sequence reduces steric and structural variability, enabling precise measurement of enzymatic parameters such as Km, Vmax, and kcat. This makes it particularly suitable for kinetic studies evaluating AMPK activation by upstream kinases (e.g., LKB1, CaMKKβ) or allosteric regulators. AMARA peptide is also employed to investigate substrate specificity and consensus motif requirements. By modifying residues flanking the serine phosphorylation site, researchers can probe the contribution of basic residues and hydrophobic determinants to kinase recognition. Comparative studies using AMARA variants help define differences between AMPK and other kinases with overlapping substrate preferences, including members of the SNF1-related kinase (SnRK) and salt-inducible kinase (SIK) families. In pharmacological research, AMARA peptide forms the basis of screening platforms for AMPK activators and inhibitors. High-throughput assays use the peptide as a standardized readout to quantify kinase activity in the presence of candidate compounds. This approach supports identification of small-molecule modulators targeting AMPK catalytic activity or upstream regulatory mechanisms. Because AMPK is implicated in metabolic disorders, cardiovascular disease, and cancer, AMARA-based assays remain central to drug discovery programs. Beyond direct kinase assays, the peptide contributes to mechanistic studies of AMPK signaling networks. By providing a controlled phosphorylation substrate, researchers can evaluate how post-translational modifications, subunit composition, or regulatory proteins influence catalytic efficiency. It also facilitates comparison between wild-type and mutant AMPK variants to assess functional consequences of disease-associated mutations. AMARA peptide has relevance in metabolic research contexts where AMPK regulates glucose uptake, fatty acid oxidation, autophagy, and mitochondrial biogenesis. Although the peptide itself does not replicate physiological substrates, it provides a reliable proxy for measuring core catalytic activity under defined experimental conditions. This is particularly valuable when dissecting upstream signaling events triggered by cellular stress, hypoxia, nutrient deprivation, or pharmacologic agents such as metformin. Overall, AMARA peptide is a minimal, well-characterized consensus substrate that enables quantitative and reproducible measurement of AMPK activity. Its defined phosphorylation motif supports detailed kinetic analysis, substrate specificity studies, and high-throughput screening applications. As a standardized tool in kinase research, it plays an important role in advancing understanding of AMPK-mediated energy sensing and metabolic signal transduction.