Recombinant Mouse Myocilin (Myoc) is produced through a baculovirus expression system and covers amino acids 213-490—a partial but substantial portion of the protein. The recombinant protein includes an N-terminal 10xHis-tag and a C-terminal Myc-tag, which streamline purification and detection processes. SDS-PAGE analysis confirms purity levels exceeding 85%. This product is designed solely for research purposes, with no established biological functions or disease connections specified.
Myocilin appears to be a protein chiefly involved in extracellular matrix processes and can be found across various tissues, particularly in the eye. The protein likely plays an important role in maintaining structural integrity and supporting cellular signaling networks. Research into myocilin seems especially relevant for ocular health studies, given its apparent association with pathways that may influence intraocular pressure and other eye-related physiological processes.
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 myocilin fragment (213-490aa) works well in pull-down assays for identifying potential binding partners in mouse ocular tissues or cell lysates. The N-terminal His-tag allows for immobilization on nickel-affinity resins. Meanwhile, the C-terminal Myc-tag provides a way to detect and confirm protein capture. Anti-Myc antibodies can be used in co-immunoprecipitation experiments to validate interactions discovered through His-tag pull-downs. This strategy appears particularly useful for investigating myocilin's role in extracellular matrix organization and cellular signaling networks.
2. Antibody Development and Validation
The recombinant myocilin fragment may serve as an immunogen for creating mouse myocilin-specific antibodies or as a control antigen when validating existing ones. The dual-tag system makes purification and detection straightforward during antibody screening. ELISA-based assays using this protein can help researchers determine antibody specificity and binding affinity. Since the fragment represents a considerable portion of the myocilin protein, it's likely suitable for developing antibodies that recognize native myocilin in tissue samples.
3. Biochemical Characterization Studies
This purified myocilin fragment opens up possibilities for detailed biochemical analysis—protein folding studies, thermal stability assessments, and structural characterization. The baculovirus expression system generally produces proteins with appropriate post-translational modifications. This makes the fragment well-suited for investigating myocilin's biochemical properties. Size exclusion chromatography, dynamic light scattering, and other biophysical techniques can help researchers understand the protein's oligomerization state and conformational characteristics. The high purity level (>85%) should ensure dependable results in quantitative biochemical assays.
4. Cell-Based Functional Assays
The tagged myocilin fragment can be introduced into cell culture experiments to examine its effects on cellular processes like extracellular matrix deposition and cell adhesion. Adding the recombinant protein to cell culture media allows researchers to monitor cellular responses while using the Myc-tag to track protein localization and uptake. The fragment might also work as a competitor in binding assays to explore myocilin's interactions with cell surface receptors or extracellular matrix components. These experiments could provide valuable insights into myocilin's biological functions in ocular tissue homeostasis.
