Activated Protein C (390-404), human is a peptide of the activated protein C (a vitamin K-dependent serine protease), potently inhibits APC anticoagulant activity.
CAT No: R1159
CAS No:146340-20-7
Synonyms/Alias:146340-20-7;L-Histidine, L-tyrosylglycyl-L-valyl-L-tyrosyl-L-threonyl-L-lysyl-L-valyl-L-seryl-L-arginyl-L-tyrosyl-L-leucyl-L-alpha-aspartyl-L-tryptophyl-L-isoleucyl- (9CI);DA-70575;FA110303;G12496;H-Tyr-Gly-Val-Tyr-Thr-Lys-Val-Ser-Arg-Tyr-Leu-Asp-Trp-Ile-His-OH; H-YGVYTKVSRYLDWIH-OH;
Activated Protein C (390-404), human, is a synthetic peptide fragment corresponding to residues 390 through 404 of the human activated protein C (APC) sequence. As a bioactive segment derived from the anticoagulant serine protease, it retains key structural motifs involved in protein-protein interactions, making it highly relevant for studies exploring the functional domains of APC and their roles in hemostasis, inflammation, and cellular signaling. The peptide's defined sequence and origin provide a targeted tool for dissecting the molecular mechanisms underlying APC-mediated physiological processes, supporting research in thrombosis, vascular biology, and peptide structure-function analysis.
Peptide interaction studies: Researchers utilize the 390-404 fragment to map and characterize binding interfaces between APC and its physiological partners. By isolating this specific domain, investigators can probe its affinity for cell surface receptors, cofactors, or inhibitors, facilitating a deeper understanding of the molecular determinants governing APC's regulatory functions. Such studies are critical for elucidating the sequence-specific contributions to substrate recognition and allosteric modulation within the broader context of the protein's activity.
Structure-function analysis: The defined peptide sequence serves as a valuable model for examining the relationship between primary structure and biological activity. Scientists employ the 390-404 fragment in mutagenesis experiments, conformational studies, and computational modeling to identify residues essential for functional integrity. Insights gained from these analyses inform the design of novel peptide analogs, contribute to structure-guided drug discovery, and enhance knowledge of the structural basis for APC's diverse physiological roles.
Anticoagulation mechanism research: The peptide is frequently used in mechanistic studies investigating the anticoagulant properties of APC. By focusing on the 390-404 region, researchers can assess its involvement in the inhibition of coagulation factors or its contribution to the modulation of thrombin generation. Such targeted studies provide clarity on how specific APC domains influence the balance between procoagulant and anticoagulant pathways, supporting the development of next-generation anticoagulant agents and informing therapeutic strategies.
Cell signaling investigations: Beyond its canonical role in coagulation, APC is implicated in a variety of cellular signaling pathways, including those regulating inflammation and apoptosis. The 390-404 fragment is employed in cell-based assays to dissect its capacity to engage with endothelial receptors or modulate intracellular signaling cascades. These experiments enable the identification of sequence motifs responsible for cytoprotective or anti-inflammatory effects, advancing the understanding of APC's pleiotropic actions at the cellular level.
Peptide synthesis and analytical validation: The human APC (390-404) fragment is also used as a standard or reference in peptide synthesis workflows and analytical method development. Its well-characterized sequence allows for the calibration of chromatographic systems, mass spectrometry protocols, and peptide purification techniques. By serving as a benchmark in these technical applications, the fragment supports quality control, method optimization, and the reliable quantification of related peptide species in complex biological samples.
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