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.
Bovine SFTPC is a lipophilic protein that requires precise folding, proper palmitoylation (a post-translational modification), and specific alpha-helical structure formation for its functional activity in lung surfactant function. The E. coli expression system cannot provide the eukaryotic folding environment or palmitoylation machinery required for this modified protein. The large N-terminal GST tag (∼26 kDa) is substantially larger than the SFTPC mature protein itself (∼4 kDa), creating severe steric interference that will completely disrupt the protein's structural organization and functional domains. The probability of correct folding with functional surfactant activity is essentially zero.
1. Antibody Development and Validation
This application has severe limitations. While antibodies can be generated, the immune response will primarily target the large foreign GST tag rather than the small SFTPC domain. Antibodies may not recognize the native, palmitoylated SFTPC in its physiological membrane-associated form.
2. GST-Tag Based Affinity Purification Studies
This application is feasible but biologically irrelevant. The protein can be used for technical GST-based purification protocols, but results will reflect GST tag behavior rather than authentic SFTPC biology. Any purified complexes will be artefactual and not representative of physiological SFTPC interactions.
Final Recommendation & Action Plan
This GST-tagged SFTPC construct is fundamentally unsuitable for meaningful SFTPC research due to the extreme size disparity between the tag (26 kDa) and the protein (4 kDa). The GST tag is over six times larger than the SFTPC domain itself, making all functional and comparative studies biologically irrelevant. The only limited application is as a technical tool for GST-based affinity methods. Avoid all interaction, comparative, and functional studies entirely. For authentic SFTPC research, use full-length protein expressed in mammalian systems that supports proper palmitoylation and preserves the protein's native membrane-associated structure and function.
