Recombinant Bovine Pulmonary surfactant-associated protein C (SFTPC) is produced in E. coli with an N-terminal GST tag, which appears to help with solubility and makes purification more straightforward. The protein represents the full length of the mature form, comprising the amino acid sequence 25-58. SDS-PAGE verification shows the product achieves a purity level exceeding 90%, which should make it suitable for sophisticated research applications.
Pulmonary surfactant-associated protein C plays a crucial role in the pulmonary surfactant system - it's essential for reducing surface tension in the lungs and preventing alveolar collapse. This protein is a vital component in respiratory research, contributing to our understanding of lung function and disorders. Its study may be significant in exploring mechanisms underlying respiratory diseases and potential therapeutic interventions.
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. In Vitro Protein-Protein Interaction Studies
This recombinant bovine SFTPC can be used to investigate protein-protein interactions within the pulmonary surfactant system through pull-down assays. The N-terminal GST tag allows for immobilization on glutathione-sepharose beads to capture potential binding partners from lung tissue lysates or purified protein preparations. The mature protein region (25-58aa) represents the biologically relevant domain that would likely interact with other surfactant proteins or lipid components under physiological conditions. This approach might help identify novel binding partners and characterize how surfactant protein complexes form at the molecular level.
2. Antibody Development and Validation
The recombinant protein serves as what appears to be an ideal antigen for generating specific antibodies against bovine SFTPC or for validating existing ones. The high purity (>90%) should minimize cross-reactivity during immunization protocols, while the GST tag can be used for affinity purification of the antigen. Researchers can use this protein in ELISA-based screening of hybridoma clones or for testing antibody specificity in Western blot applications. The defined expression region (25-58aa) allows for precise epitope mapping studies to determine where antibodies bind.
3. Comparative Species Analysis in Surfactant Research
This bovine SFTPC can be used in comparative studies examining species-specific differences in pulmonary surfactant protein structure and function across mammalian models. Researchers can perform side-by-side biochemical analyses comparing bovine SFTPC with human or other species variants to understand evolutionary conservation and divergence. The standardized expression system and purification approach should enable consistent preparation for cross-species binding studies or structural comparisons using techniques such as circular dichroism spectroscopy.
4. GST-Tag Based Affinity Purification Studies
The N-terminal GST tag makes this protein suitable for developing affinity purification protocols to isolate SFTPC-associated complexes from biological samples. Researchers can use glutathione affinity chromatography to capture protein complexes or study how SFTPC binds with lipid vesicles or other surfactant components. This application may be particularly valuable for biochemical characterization studies where the GST tag provides a reliable handle for protein immobilization and subsequent analysis of bound materials.
