Kallikrein-4 (155-169)

Kallikrein-4 (155-169) is a synthetic peptide fragment derived from the human kallikrein-4 protein, a member of the tissue kallikrein family of serine proteases. This peptide represents a defined sequence within the C-terminal region of kallikrein-4, which is implicated in various physiological and pathological processes, including extracellular matrix remodeling, cell signaling, and proteolytic cascades. Due to its well-characterized amino acid sequence and relevance to protease biology, Kallikrein-4 (155-169) serves as a valuable tool in biochemical research focused on understanding substrate specificity, protein-protein interactions, and regulatory mechanisms involving kallikrein family members.

Enzymology studies: Researchers employ this peptide fragment in enzymology assays to investigate the substrate recognition and cleavage specificity of kallikrein-4 and related serine proteases. By providing a defined substrate or competitive inhibitor, the peptide allows detailed kinetic analyses and mapping of active site preferences, contributing to a deeper understanding of proteolytic activity and regulation within the kallikrein family.

Protease inhibitor screening: The peptide is frequently utilized in high-throughput screening platforms designed to identify and characterize inhibitors of kallikrein-4 activity. Through monitoring the hydrolysis or binding of the peptide sequence, scientists can evaluate the efficacy and selectivity of candidate inhibitors, advancing the discovery of novel modulators for biochemical and pharmacological research.

Protein interaction mapping: Kallikrein-4 (155-169) is valuable in studies aimed at elucidating protein-protein interaction networks involving kallikrein-4. By serving as a molecular probe, the peptide facilitates affinity-based assays such as pull-downs or surface plasmon resonance, enabling the identification of binding partners and interaction domains relevant to extracellular matrix dynamics and cell signaling pathways.

Antibody development and validation: Synthetic peptides corresponding to unique protein regions are widely employed as immunogens or assay standards in antibody production. The defined sequence of this peptide fragment supports the generation and validation of highly specific antibodies against kallikrein-4, which are essential for immunodetection, quantification, and localization studies in tissue samples or cell lysates.

Mass spectrometry calibration: The peptide's precise amino acid composition makes it an ideal standard for calibrating and validating mass spectrometry-based proteomic workflows. By incorporating Kallikrein-4 (155-169) as a reference or spike-in control, researchers can ensure accurate mass determination, optimize peptide fragmentation parameters, and improve the reliability of protein identification and quantification in complex biological samples.

1. Application of human liver organoids as a patient-derived primary model for HBV infection and related hepatocellular carcinoma

2. Glucagonlike peptide 2 analogue teduglutide: stimulation of proliferation but reduction of differentiation in human Caco-2 intestinal epithelial cells

3. Effect of Short-Term Desiccation, Recovery Time, and CAPA-PVK Neuropeptide on the Immune System of the Burying Beetle Nicrophorus vespilloides

4. Sex differences in oxidative stress level and antioxidative enzymes expression and activity in obese pre-diabetic elderly rats treated with metformin or liraglutide

5. Cationic cell-penetrating peptides are potent furin inhibitors