Recombinant Human Extracellular serine/threonine protein kinase FAM20C is produced in a mammalian expression system, which appears to ensure proper folding and post-translational modifications. This partial protein covers amino acids 354 to 565. It's tagged with an N-terminal 10xHis-tag and a C-terminal Myc-tag for easier purification and detection. The product shows purity greater than 85%, as verified by SDS-PAGE, making it suitable for various biochemical assays and research applications.
FAM20C is a serine/threonine protein kinase that plays a crucial role in the phosphorylation of extracellular proteins. It's known for its involvement in biomineralization processes and regulating the secretion of phosphoproteins. As a key component of the secretory pathway, FAM20C modulates the phosphorylation status of proteins, influencing numerous biological pathways. This makes it an important target for research in cellular signaling and disease mechanisms.
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.
The recombinant human FAM20C fragment (354–565aa), expressed in mammalian cells with N-terminal 10xHis and C-terminal Myc tags, represents a partial segment of the full-length kinase, which spans approximately 584 amino acids. This region lies within the core catalytic domain of FAM20C, an extracellular serine/threonine kinase responsible for phosphorylating secreted proteins. Because the fragment originates from a mammalian expression system, it is likely to undergo correct folding and glycosylation, ensuring near-native conformation. However, since the fragment does not include the complete catalytic domain (lacking N-terminal residues that contribute to ATP binding and substrate recognition), it is unlikely to retain full enzymatic activity. Therefore, the protein is probably well-folded structurally but catalytically inactive or only partially active. It remains suitable for structural, antibody, and binding studies, but not for reliable kinase activity assays without validation.
1. Protein-Protein Interaction Studies
This dual-tagged FAM20C fragment (354–565aa) can be applied in pull-down or affinity-based assays to identify potential interacting proteins that bind within this region of FAM20C. If properly folded—as expected from mammalian expression—it may preserve native-like interaction surfaces, allowing meaningful mapping of partial binding interfaces. If the fragment lacks structural integrity or the N-terminal interaction determinants, it can still serve for screening studies or linear epitope-based binding assays, though such results would need cautious interpretation. Overall, it is useful for preliminary interaction screening but not for reconstructing full enzymatic interaction networks.
2. Antibody Development and Validation
This recombinant fragment is suitable as an antigen for generating antibodies against the 354–565aa region of human FAM20C. If correctly folded, antibodies may recognize native epitopes of the kinase domain, making them valuable for immunostaining or immunoprecipitation. If folding deviates, antibodies would instead recognize linear epitopes, which are still suitable for Western blot and ELISA detection. The dual-tag design facilitates both purification and validation during antibody development and ensures straightforward quality control of immunogens.
3. Structural and Biochemical Characterization
This FAM20C fragment may be used for biophysical and structural characterization of the kinase region. If folded properly, it could serve in CD spectroscopy, DLS, and limited proteolysis to examine secondary structure content and domain stability. If the protein lacks catalytic residues, it remains useful for folding and conformation studies but not for functional enzymatic characterization. The mammalian expression system provides a strong foundation for studying native-like folding, even if activity is lost due to truncation.
Thus, this application requires explicit experimental confirmation of activity before functional interpretation.
Final Recommendation & Action Plan
The recombinant FAM20C fragment expressed in mammalian cells is structurally reliable but catalytically incomplete. Its folding is likely accurate, making it suitable for antibody generation, interaction mapping, and structural or stability assays. However, due to the truncation within the kinase domain, it should not be used as an active kinase without functional validation. Employ this protein for binding and structural characterization, validate folding via CD or limited proteolysis, and only use it in in vitro kinase assays as a test construct with clear caveats about potential inactivity. For catalytic or mechanistic studies, use full-length or extended constructs encompassing the complete kinase domain.
