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.
1. Protein-Protein Interaction Studies
This dual-tagged FAM20C fragment can be used in pull-down assays to identify potential binding partners or substrates of the FAM20C kinase domain. The N-terminal His-tag enables immobilization on nickel-based resins. Meanwhile, the C-terminal Myc-tag helps with detection and validation of interactions through Western blotting or immunofluorescence. The mammalian expression system likely ensures proper protein folding and post-translational modifications that may be critical for physiologically relevant interactions. Such studies could help clarify the molecular mechanisms underlying FAM20C function in cellular signaling pathways.
2. Antibody Development and Validation
The recombinant FAM20C protein can serve as an antigen for generating specific antibodies against the 354-565 amino acid region of human FAM20C. The dual-tag system allows for easy purification and quality control during antibody production and screening processes. Researchers can use this protein to validate antibody specificity through ELISA, Western blot, and immunoprecipitation assays. The high purity level (>85%) should minimize cross-reactivity during antibody development and characterization.
3. Structural and Biochemical Characterization
This partial FAM20C protein fragment can be used in biophysical studies to investigate the structural properties of the kinase domain region. The protein may work well in techniques such as circular dichroism spectroscopy, dynamic light scattering, or analytical ultracentrifugation to assess protein stability, folding, and oligomerization states. The mammalian expression system provides appropriately folded protein that may retain native-like conformational features essential for accurate structural analysis.
4. In Vitro Kinase Assay Development
Although biological activity has not been tested, this FAM20C fragment containing the kinase domain region can be used to establish and optimize in vitro kinase assay protocols. Researchers can test various substrate candidates and reaction conditions to determine optimal parameters for kinase activity measurements. The dual-tag system helps with protein immobilization and detection in assay formats, enabling the development of standardized protocols for future FAM20C functional studies.
