This multi-residue peptide contains hydrophobic clusters, polar segments, and aromatic residues that enable diverse secondary-structure formation. Researchers employ it to map folding thermodynamics, solvent-dependent transitions, and peptide-protein interfaces. The sequence's distribution of acidic and basic residues supports electrostatic modulation studies. Its length facilitates in-depth biophysical surveys.
CAT No: R2412
CAS No:880150-82-3
Synonyms/Alias:H-Arg-Met-Asn-Ile-Gln-Met-Leu-Leu-Glu-Ala-Ala-Asp-Tyr-Leu-Glu-Arg-OH;Mad1 (6-21);880150-82-3;AKOS040758428;DA-65198;
H-Arg-Met-Asn-Ile-Gln-Met-Leu-Leu-Glu-Ala-Ala-Asp-Tyr-Leu-Glu-Arg-OH is a synthetic peptide sequence designed to facilitate advanced research in the fields of biochemistry, molecular biology, and cellular signaling. Characterized by its precise amino acid arrangement, this peptide offers a valuable tool for probing protein-protein interactions, studying receptor binding affinities, and elucidating intracellular pathways. Its unique sequence enables researchers to investigate structural motifs critical for biological activity, while its stability and solubility in aqueous environments make it particularly suitable for a range of experimental protocols. As a research-grade peptide, it provides flexibility for customization and can be adapted for use in diverse scientific applications, supporting innovation in both academic and industrial settings.
Protein-Protein Interaction Studies: H-Arg-Met-Asn-Ile-Gln-Met-Leu-Leu-Glu-Ala-Ala-Asp-Tyr-Leu-Glu-Arg-OH is widely utilized in the exploration of protein-protein interactions, serving as a model substrate or ligand in binding assays. By incorporating this peptide into pull-down experiments or surface plasmon resonance analyses, researchers can map interaction domains, quantify binding affinities, and identify novel partners involved in complex signaling pathways. Its defined sequence enables precise manipulation, allowing for structure-activity relationship studies that shed light on the molecular determinants of protein recognition and assembly.
Signal Transduction Research: In the context of intracellular signaling, this peptide is employed to dissect the roles of specific motifs in activating or inhibiting downstream pathways. By introducing it into cultured cells or cell-free systems, investigators can observe its effects on phosphorylation cascades, second messenger production, and gene expression patterns. The sequence's resemblance to native protein segments makes it an effective competitive inhibitor or agonist, enabling the dissection of pathway specificity and the identification of critical regulatory checkpoints.
Enzyme Substrate Characterization: As a synthetic peptide, H-Arg-Met-Asn-Ile-Gln-Met-Leu-Leu-Glu-Ala-Ala-Asp-Tyr-Leu-Glu-Arg-OH is frequently used as a substrate in enzymatic assays designed to characterize proteases, kinases, or other modifying enzymes. By monitoring cleavage or modification events, researchers can determine substrate specificity, kinetic parameters, and inhibitory profiles. This information is invaluable for the development of targeted inhibitors or the optimization of enzyme-based biotechnological processes, offering insights into both fundamental biochemistry and applied research.
Antibody Production and Epitope Mapping: The unique sequence of this peptide allows for its use in generating sequence-specific antibodies, which are essential for detecting and quantifying target proteins in complex biological samples. By immunizing animals with the peptide or employing it in affinity purification protocols, scientists can obtain high-affinity antibodies for use in Western blotting, immunohistochemistry, or ELISA. Additionally, mapping antibody binding to this sequence helps define antigenic determinants, supporting the development of diagnostic reagents and advancing our understanding of immune recognition.
Peptide-Based Biosensor Development: H-Arg-Met-Asn-Ile-Gln-Met-Leu-Leu-Glu-Ala-Ala-Asp-Tyr-Leu-Glu-Arg-OH also finds application in the creation of biosensors for the detection of specific biomolecules or environmental changes. By immobilizing the peptide on sensor surfaces, researchers can exploit its binding properties to develop sensitive and selective detection platforms. These biosensors are valuable for real-time monitoring of biochemical interactions, environmental contaminants, or disease biomarkers, driving advancements in analytical technology and applied life sciences.
Through its multifaceted applications, H-Arg-Met-Asn-Ile-Gln-Met-Leu-Leu-Glu-Ala-Ala-Asp-Tyr-Leu-Glu-Arg-OH supports a wide array of research endeavors, from unraveling the complexities of cellular communication to enabling the development of innovative analytical tools. Its versatility and well-defined structure make it an indispensable reagent for scientists seeking to advance knowledge in molecular biology, biochemistry, and related disciplines.
2. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
5. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
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