Kallikrein-4 (160-174)

Kallikrein-4 (160-174) is a synthetic peptide fragment derived from the human tissue kallikrein-4 serine protease, corresponding to amino acids 160 through 174 of the parent protein. As a peptide compound, it represents a defined sequence within the kallikrein-4 enzyme, which is known for its involvement in proteolytic pathways and regulatory processes in various tissues. The 160-174 fragment is of particular interest due to its potential to model specific functional domains, enabling researchers to dissect the biochemical interactions and substrate specificities associated with the kallikrein-4 family. Its defined structure and origin make it a valuable tool for investigating peptide-protein interactions, enzymatic mechanisms, and the broader physiological roles of kallikrein-related peptides in biological systems.

Peptide-Protein Interaction Studies: The 160-174 fragment of kallikrein-4 serves as a precise molecular probe for exploring peptide-protein interactions relevant to serine protease biology. Researchers utilize this peptide to map binding sites, characterize interaction partners, and study the structural determinants that govern substrate recognition within the kallikrein-4 enzyme family. By enabling targeted binding assays and affinity studies, the peptide facilitates a deeper understanding of how specific regions within kallikrein-4 contribute to its regulatory and catalytic functions.

Enzymatic Mechanism Elucidation: As a segment corresponding to an active region of kallikrein-4, the peptide is employed in mechanistic studies aimed at dissecting the catalytic processes of serine proteases. It can be used as a substrate mimic or competitive inhibitor in in vitro assays to analyze cleavage specificity, enzyme kinetics, and the effects of sequence modifications on proteolytic activity. These applications are essential for elucidating the molecular underpinnings of kallikrein-mediated proteolysis and for informing the design of selective modulators or inhibitors.

Peptide Structure-Function Analysis: The defined sequence of kallikrein-4 (160-174) allows for systematic structure-activity relationship (SAR) studies, where researchers investigate how specific amino acid residues contribute to the peptide's conformational stability and biological activity. By subjecting the peptide to modifications or labeling, it becomes possible to probe secondary structure, folding dynamics, and functional motifs. Such analyses are critical for understanding the structural requirements for peptide-mediated interactions and for guiding the development of optimized analogs for research use.

Biochemical Assay Development: The peptide fragment is frequently incorporated into assay platforms designed to monitor protease activity, screen for enzyme modulators, or validate antibody specificity. Its well-defined sequence and origin from a biologically relevant protease make it a reliable standard or control in biochemical assays. Use in ELISA, Western blotting, or mass spectrometry-based methods enables precise quantification and detection of kallikrein-related activity, supporting robust assay development in both academic and industrial research settings.

Peptide Synthesis and Analytical Validation: Kallikrein-4 (160-174) is also valuable as a reference standard in peptide synthesis workflows and analytical validation. Synthetic chemists and analytical biochemists employ the peptide to calibrate instrumentation, validate chromatographic methods, and assess peptide purity or sequence integrity. Its role as a benchmark compound ensures reproducibility and accuracy in peptide manufacturing and quality control processes, supporting the broader field of peptide-based research and development.

1. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists

2. Crystal Structure of BamB from Pseudomonas aeruginosa and Functional Evaluation of Its Conserved Structural Features

3. Multifunctional peptide-oligonucleotide conjugate promoted sensitive electrochemical biosensing of cardiac troponin I

4. The effect of sex on immune responses to a homocitrullinated peptide in the DR4-transgenic mouse model of Rheumatoid Arthritis

5. An interdomain binding site on HIV-1 Nef interacts with PACS-1 and PACS-2 on endosomes to down-regulate MHC-I