SAMS Peptide [HMRSAMSGLHLVKRR-NH2]

Product Name: SAMS Peptide [HMRSAMSGLHLVKRR-NH2]

Sequence One Letter Code: HMRSAMSGLHLVKRR-NH2

Sequence Three Letter Code: H-His-Met-Arg-Ser-Ala-Met-Ser-Gly-Leu-His-Leu-Val-Lys-Arg-Arg-NH2

Chemical Formula:C74H132N30O17S2

Molecular Weight: 1778.3

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: peptide substrate

Conjugation: Unconjugated

Code Nacres: NA.26

Application: SAMS Peptide is a synthetic peptide substrate with the sequence HMRSAMSGLHLVKRR-NH₂, specifically designed for selective measurement of AMP-activated protein kinase (AMPK) activity. AMPK functions as a master regulator of cellular energy homeostasis, becoming activated in response to increased AMP/ATP ratios during metabolic stress. The SAMS motif within this peptide contains the consensus phosphorylation site efficiently recognized by AMPK, enabling highly specific and reproducible phosphorylation in vitro. SAMS Peptide is widely employed in radiometric, colorimetric, and fluorescence-based kinase assays to quantify AMPK catalytic activity. It supports kinetic characterization, substrate affinity analysis, and high-throughput screening of AMPK modulators. Because AMPK signaling is central to metabolic regulation, mitochondrial function, and glucose homeostasis, this peptide substrate serves as a valuable biochemical tool in studies of metabolic disorders, obesity, diabetes, and AMPK-targeted therapeutic development in academic and pharmaceutical research settings.

Current Research: SAMS Peptide is a synthetic peptide substrate with the sequence HMRSAMSGLHLVKRR-NH₂, specifically developed for selective measurement of AMP-activated protein kinase (AMPK) activity. AMPK is a serine/threonine kinase that functions as a central regulator of cellular energy balance, becoming activated in response to elevated AMP/ATP or ADP/ATP ratios during metabolic stress. Once activated, AMPK orchestrates adaptive responses that restore energy homeostasis by promoting catabolic pathways and suppressing anabolic processes. The SAMS motif embedded within this peptide contains a well-characterized consensus phosphorylation site that is efficiently and preferentially recognized by AMPK. This sequence enables robust and reproducible phosphorylation in vitro, providing a reliable readout of AMPK catalytic activity. The C-terminal amidation enhances peptide stability and more closely mimics native substrate features, contributing to consistent assay performance across experimental platforms. SAMS Peptide has become a widely accepted reference substrate in biochemical assays designed to quantify AMPK activity. It is compatible with multiple detection formats, including radiometric assays using γ-³²P-ATP incorporation, colorimetric kinase assays, and fluorescence-based systems that detect phosphate transfer or downstream signal generation. This flexibility allows researchers to tailor assay design to specific sensitivity requirements, throughput needs, or instrumentation availability. In kinetic studies, SAMS Peptide supports determination of key enzymatic parameters such as Km and Vmax, enabling detailed characterization of AMPK catalytic efficiency under varying conditions. It is also suitable for evaluating substrate competition and ATP dependency, facilitating mechanistic insights into enzyme regulation. Because of its defined sequence and predictable phosphorylation behavior, the peptide provides a standardized platform for comparing AMPK activity across cell lysates, recombinant protein preparations, or purified kinase complexes. Beyond basic enzymology, SAMS Peptide plays an important role in high-throughput screening workflows. It is frequently employed in compound screening campaigns aimed at identifying AMPK activators or inhibitors. The robust phosphorylation signal generated by AMPK in the presence of SAMS Peptide ensures strong assay windows and reproducible performance, supporting reliable detection of pharmacological modulation. This makes it particularly valuable in early-stage drug discovery and target validation programs focused on metabolic disease intervention. AMPK signaling is deeply integrated into pathways governing glucose uptake, lipid oxidation, mitochondrial biogenesis, and autophagy. Dysregulation of AMPK activity has been associated with metabolic disorders such as obesity, type 2 diabetes, and non-alcoholic fatty liver disease, as well as with broader processes including aging and cellular stress adaptation. As a result, precise measurement of AMPK activity is critical for understanding disease mechanisms and evaluating therapeutic strategies. SAMS Peptide provides a direct biochemical tool for assessing AMPK function in both academic and pharmaceutical research settings. It enables quantification of kinase activation in response to metabolic stressors, pharmacological agents, or genetic manipulation. When combined with upstream activation studies—such as analysis of LKB1 or CaMKK2-mediated phosphorylation—SAMS-based assays contribute to a comprehensive evaluation of AMPK pathway dynamics. In summary, SAMS Peptide is a highly specific and dependable substrate for AMPK activity measurement. Its optimized consensus sequence, compatibility with diverse assay formats, and suitability for kinetic and screening applications make it a foundational reagent in metabolic research. By supporting accurate and reproducible evaluation of AMPK catalytic function, SAMS Peptide facilitates mechanistic studies and therapeutic development targeting cellular energy regulation.