NH2-QGGYTMHQDQEGDTDAGLK-COOH is a synthetic peptide chain with an amine group attached to lysine and an carboxyl group attached to glutamine.
CAT No: R1558
NH2-KLGADTDGEQDQHMTYGGQ-COOH is a synthetic peptide sequence designed for advanced biochemical and molecular research applications. As a custom peptide with a defined N-terminal amine and C-terminal carboxyl group, it offers precise control over its structural and functional properties. The sequence itself may be derived from or modeled after biologically relevant regions of target proteins, enabling researchers to explore specific protein-protein interactions, post-translational modifications, or signal transduction pathways. Its utility in experimental design stems from its high sequence fidelity, making it suitable for a wide range of peptide-centric investigations in both basic and applied sciences.
Peptide-protein interaction studies: Researchers frequently utilize this peptide to dissect the molecular basis of protein-protein interactions. By incorporating the sequence into binding assays, pull-down experiments, or surface plasmon resonance analyses, investigators can map interaction domains, characterize binding affinities, and identify critical residues involved in complex formation. Such studies are instrumental in elucidating signaling cascades, scaffolding functions, and regulatory mechanisms within cellular systems.
Epitope mapping and antibody validation: The defined sequence of NH2-KLGADTDGEQDQHMTYGGQ-COOH makes it a valuable tool for epitope mapping and antibody specificity testing. Synthetic peptides are often employed to determine the precise binding sites of monoclonal or polyclonal antibodies, facilitating the development of highly specific immunoassays. By immobilizing the peptide on solid supports or using it in competitive binding formats, researchers can confirm antibody recognition and minimize cross-reactivity, thereby improving assay reliability.
Peptide substrate assays: The sequence can serve as a substrate in enzymatic assays designed to measure the activity of proteases, kinases, or other modifying enzymes. By monitoring cleavage, phosphorylation, or other modifications of the peptide, scientists can quantify enzyme kinetics, assess inhibitor potency, or screen for modulators of enzymatic function. This approach provides a controlled system for dissecting enzyme specificity and mechanism, supporting drug discovery and functional proteomics.
Structural and conformational analysis: Synthetic peptides like NH2-KLGADTDGEQDQHMTYGGQ-COOH are frequently used in studies aimed at understanding secondary structure formation, folding dynamics, or aggregation behavior. Techniques such as circular dichroism spectroscopy, NMR, or X-ray crystallography can be applied to the peptide to reveal its conformational preferences and to model its behavior within larger protein complexes. Insights gained from such analyses contribute to the broader understanding of protein architecture and stability.
Peptide-based assay development: The sequence is well suited for incorporation into custom assay platforms, including ELISA, fluorescence-based detection systems, and biosensor technologies. By leveraging its defined chemical characteristics, researchers can tailor detection schemes, optimize assay sensitivity, and calibrate quantitative measurements. Such applications are particularly relevant for high-throughput screening, biomarker discovery, and the development of diagnostic research tools, where reproducibility and specificity are paramount.
2. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis
3. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
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