Recombinant Human C-C motif chemokine 27 protein (CCL27) is produced in an E. coli expression system, spanning the full mature protein from amino acids 25 to 112. This tag-free protein maintains a high purity level of over 96% as verified by SDS-PAGE analysis. It displays significant biological activity, confirmed via a chemotaxis bioassay with CCR10 transfected BaF3 cells, within a concentration range of 10-100 ng/ml. The endotoxin level is controlled to less than 1.0 EU/µg, as determined by the LAL method.
CCL27 appears to function as a chemokine within the immune system's signaling networks. It likely plays a critical role in directing immune cell movement toward inflammation sites, particularly affecting skin tissue where it interacts with the receptor CCR10. Understanding CCL27 may be vital for researchers investigating immune response mechanisms and potential therapeutic targets in inflammatory conditions.
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. CCR10 Receptor Binding and Signaling Studies
This recombinant CCL27 protein can investigate the binding kinetics and signaling pathways mediated by the CCR10 receptor in transfected cell lines. The confirmed biological activity in CCR10-transfected BaF3 cells at 10-100 ng/ml concentrations makes it suitable for dose-response studies and receptor characterization experiments. Researchers might use this protein to study downstream signaling cascades, including calcium mobilization assays and cAMP measurements in CCR10-expressing cells.
2. Chemotaxis and Cell Migration Assays
The demonstrated chemotactic activity suggests this CCL27 protein could serve as an excellent tool for studying directional cell migration in vitro. Transwell migration assays, Boyden chamber experiments, or microfluidic devices may be used to analyze the migratory behavior of CCR10-positive cells, including skin-homing T cells and other immune cell populations. The defined active concentration range provides a reliable starting point for establishing optimal experimental conditions.
3. Antibody Development and Validation
This high-purity, tag-free CCL27 protein serves as what appears to be an ideal antigen for generating and validating anti-CCL27 antibodies. The >96% purity and low endotoxin levels make it suitable for immunization protocols and subsequent antibody screening assays. The protein can also function as a positive control in ELISA, Western blot, and immunoprecipitation experiments to validate antibody specificity and sensitivity.
4. Protein-Protein Interaction Studies
The biologically active CCL27 protein can be applied in binding assays to identify and characterize interactions with potential binding partners beyond CCR10. Surface plasmon resonance, bio-layer interferometry, or co-immunoprecipitation experiments may be performed to study binding affinities and kinetics with various proteins. The tag-free nature eliminates potential interference from fusion tags in these interaction studies.
5. Structure-Function Relationship Analysis
This recombinant CCL27 protein can serve as a reference standard for comparative studies with mutant or modified versions of the chemokine. Researchers might use it alongside engineered variants to assess how specific amino acid changes affect biological activity, receptor binding, or protein stability. The well-characterized activity profile provides a baseline for evaluating the functional consequences of structural modifications.
