Recombinant Human Membrane Protein MLC1-VLPs are produced using a mammalian cell expression system, spanning the full-length protein from amino acid 1 to 377. The product carries a C-terminal 10xHis-tag, which appears suitable for testing under denaturing conditions. This protein comes in the form of virus-like particles (VLPs) and contains eight transmembrane domains, which likely helps maintain structural integrity for research applications.
MLC1 is a membrane protein found in humans that participates in various cellular processes. It seems to play a critical role in maintaining nervous system function. Researchers frequently examine this protein in neurological studies, since it's a cellular membrane component that may have important implications in cellular signaling pathways.
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.
Based on the provided information, the recombinant Human MLC1 is expressed as virus-like particles (VLPs) in a mammalian cell system, a highly advantageous approach for producing complex membrane proteins with multiple transmembrane domains. The mammalian expression system typically provides the proper cellular machinery for correct folding, post-translational modifications, and membrane integration. The VLP format preserves the native membrane context, further supporting proper protein folding and orientation. While activity is unverified, the expression system and presentation method significantly increase the probability that the protein is correctly folded. However, without specific functional validation (e.g., ion channel activity or confirmed protein interactions for MLC1), bioactivity cannot be guaranteed.
1. Membrane Protein Expression and Folding Studies
This application is well-supported. The VLP platform, combined with mammalian expression, provides an excellent model for studying membrane protein folding and stability. The system likely maintains the native conformation of this 8-transmembrane protein, making it suitable for investigating folding efficiency and the effects of mutations.
2. Antibody Development and Epitope Mapping
This application is highly suitable. The VLP-presented MLC1 should display native conformational epitopes, making it an ideal immunogen for generating conformation-specific antibodies. The mammalian expression system ensures proper post-translational modifications. This represents a significant advantage over denatured or bacterially expressed protein for antibody development.
3. Membrane Protein-Lipid Interaction Studies
The VLP format is appropriate for studying protein-lipid interactions in a native membrane environment. However, the lipid composition of VLPs is typically determined by the host cell and may not be easily modifiable. While the application is feasible for studying interactions with native lipids, reconstituting VLPs in various lipid compositions may be technically challenging and requires validation. The concept is valid but may have practical limitations.
4. Protein-Protein Interaction Screening in Membrane Context
This application is theoretically possible but has significant limitations. While the VLP format preserves membrane context, the note that the C-terminal His-tag is "only functional under denaturing conditions" severely restricts its utility for pull-down assays or immobilization strategies under native conditions. This makes standard interaction screening approaches problematic. Alternative methods not requiring tag-based immobilization would be necessary.
Final Recommendation & Action Plan
Given the high likelihood of proper folding due to the mammalian-VLP expression system, this MLC1 protein is particularly valuable for structural studies, antibody development, and protein-lipid interaction research. However, the lack of activity validation necessitates caution for functional studies. The recommended plan is to first perform basic characterization to confirm membrane integration and oligomeric state (e.g., blue native PAGE, electron microscopy). For protein-protein interaction studies, alternative approaches such as cross-linking mass spectrometry or fluorescence-based assays that don't require tag accessibility under native conditions should be considered. The product appears excellent for applications 1-3, while application 4 would require significant methodological adaptation or validation with orthogonal techniques.
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