PM 102 is heparin antagonist that reverses the anticoagulant effect of heparin and potently binds heparin (Kd = 36 nM in vitro).
PM 102 is a synthetic peptide compound widely recognized for its utility in peptide-based research and biochemical investigations. As a sequence-defined peptide, it is engineered to support a range of experimental applications where precise molecular interactions are critical. Its defined structure and reproducibility make it a valuable tool for researchers seeking to elucidate peptide function, probe protein-peptide interactions, or develop novel assay systems. The compound's stability and compatibility with standard laboratory protocols further enhance its relevance across diverse fields such as molecular biology, biochemistry, and pharmaceutical research.
Peptide mapping: In proteomic and analytical workflows, PM 102 serves as a reliable standard or probe for peptide mapping studies. Its well-characterized sequence allows researchers to calibrate and validate mass spectrometry or chromatographic methods. Utilizing this peptide, scientists can assess method performance, optimize separation conditions, and ensure accurate identification of peptide fragments in complex biological samples. Such mapping efforts are crucial for characterizing post-translational modifications, verifying protein identity, and supporting quality control in peptide synthesis or biopharmaceutical production.
Protein-peptide interaction studies: The defined structure of PM 102 makes it particularly suitable for investigating protein-peptide interactions. In binding assays, surface plasmon resonance, or isothermal titration calorimetry, it can be used to quantify binding affinities, map interaction domains, or screen for modulators of protein function. These studies yield insights into molecular recognition events that underlie signal transduction, regulatory mechanisms, or the development of peptide-based inhibitors and mimetics.
Enzyme substrate analysis: PM 102 can be employed as a model substrate in enzymatic assays designed to characterize protease specificity and activity. By monitoring the hydrolysis or modification of the peptide, researchers can determine kinetic parameters, identify cleavage sites, and evaluate the selectivity of enzyme inhibitors. Such applications are instrumental in drug discovery efforts, functional annotation of proteolytic enzymes, and the development of diagnostic assays that rely on peptide substrates.
Cell signaling research: In cellular and molecular biology, synthetic peptides like PM 102 are often used to probe signaling pathways or modulate specific biological processes. By introducing the peptide into cultured cells or biochemical systems, investigators can assess its impact on receptor activation, downstream signaling events, or cellular phenotypes. These experiments facilitate the identification of critical signaling nodes, the validation of drug targets, and the exploration of peptide-mediated modulation of cellular functions.
Assay development and optimization: PM 102 is frequently utilized in the development and optimization of quantitative and qualitative assays. Its defined composition and stability enable its use as a positive control, reference standard, or calibration tool in ELISA, fluorescence-based assays, or high-throughput screening platforms. Incorporating such peptides into assay systems enhances reproducibility, supports method validation, and ensures the reliability of experimental data across multiple research and industrial contexts.
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