Recombinant Mouse Platelet factor 4 protein (Pf4) is produced in E. coli and represents the full length of the mature protein, spanning amino acids 30-105. This tag-free protein reaches purification levels greater than 97% as determined by SDS-PAGE analysis. It maintains biological activity, which appears to be confirmed by a chemotaxis bioassay using human neutrophils within a concentration range of 10-100 ng/ml. The endotoxin level remains strictly controlled, staying below 1.0 EU/µg as verified by the LAL method.
Platelet factor 4 (Pf4) is a chemokine mainly released by platelets during coagulation. It likely plays a crucial role in modulating the immune response by influencing neutrophil activity and other leukocyte functions. Pf4 appears to be involved in various biological pathways, including inflammation and wound healing processes. Its significance in research stems from its involvement in these critical physiological and pathological pathways, making it an essential protein for investigation in immunological studies.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
1. Neutrophil Chemotaxis Assays and Migration Studies
This recombinant mouse Pf4 protein can serve as a positive control or test reagent in neutrophil chemotaxis assays, given its demonstrated biological activity in promoting human neutrophil migration at concentrations of 10-100 ng/ml. Researchers can work with this protein to study neutrophil recruitment mechanisms and compare chemotactic responses across different experimental conditions. The high purity (>97%) and low endotoxin levels make it suitable for cell-based assays where contamination could confound results. This application is directly supported by the provided activity testing method. It may also be extended to investigate species-specific differences in neutrophil responses.
2. Comparative Protein Structure-Function Analysis
The tag-free nature and high purity of this recombinant mouse Pf4 protein make it valuable for biochemical characterization studies comparing mouse and human platelet factor 4 proteins. Researchers can perform binding assays, protein-protein interaction studies, and structural analyses to understand species-specific differences in Pf4 function. The mature protein region (30-105aa) represents the biologically relevant form, which appears to allow for accurate comparative studies with other species variants. Such research may provide insights into evolutionary conservation of Pf4 function across mammalian species.
3. Antibody Development and Validation
This highly pure, biologically active mouse Pf4 protein can serve as an antigen for generating species-specific antibodies or as a standard for validating existing anti-Pf4 antibodies. The low endotoxin content ensures reliable immunization protocols for antibody production. Researchers can work with this protein in ELISA development, Western blot validation, and specificity testing of Pf4-targeting antibodies. The confirmed biological activity provides an additional parameter for validating antibodies intended for functional studies.
4. Heparin-Binding and Glycosaminoglycan Interaction Studies
Given that platelet factor 4 is known to interact with heparin and other glycosaminoglycans, this recombinant protein can be used in binding assays to characterize these interactions in the mouse system. Researchers can perform surface plasmon resonance, ELISA-based binding assays, or gel shift assays to study the affinity and specificity of mouse Pf4 for various glycosaminoglycans. The high purity and biological activity of this protein suggests it should provide reliable and reproducible binding data. Such studies may contribute to understanding species-specific differences in Pf4-glycosaminoglycan interactions.
5. Preclinical Research Model Development
This biologically active mouse Pf4 protein can be used in preclinical research studies with mouse models to investigate platelet factor 4 function in various pathological contexts. The protein can serve as a positive control in studies examining inflammatory responses, wound healing, or vascular biology where Pf4 plays a role. Researchers can work with this protein to supplement or modulate endogenous Pf4 levels in experimental systems. The demonstrated neutrophil chemotactic activity provides a measurable endpoint for validating the protein's function in complex biological systems.
