Recombinant Mouse B-lymphocyte antigen CD20 (Ms4a1) is produced through a yeast expression system, targeting amino acid residues 132-291. This partial protein comes with an N-terminal 6xHis-tag, which streamlines purification processes. SDS-PAGE analysis confirms purity levels exceeding 90%, suggesting this protein offers dependable quality for research applications. The product is designed exclusively for research purposes and should not be considered for therapeutic applications.
CD20 appears to be a cell surface molecule found mainly on B-lymphocytes. It seems to play an important role in B-cell development and differentiation. Research indicates CD20 may be involved in signal transduction pathways that control cell cycle progression and proliferation. Studies examining CD20 interactions and functions are likely crucial for advancing immunology and hematological research.
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. Anti-CD20 Antibody Development and Characterization
This recombinant mouse CD20 protein fragment may serve as an antigen for creating antibodies against mouse CD20 in laboratory settings. The N-terminal His-tag appears to simplify purification and allows attachment to different surfaces during immunization protocols or screening assays. Scientists might find this protein useful for developing monoclonal or polyclonal antibodies specific to mouse CD20 for flow cytometry, immunohistochemistry, or Western blot work in murine B-cell studies. The high purity (>90%) suggests minimal contamination that could potentially disrupt antibody specificity.
2. Protein-Protein Interaction Studies
Scientists could use the His-tagged mouse CD20 fragment in pull-down assays to discover possible binding partners or interacting proteins in mouse B-cell lysates. The His-tag enables straightforward attachment to nickel-based affinity matrices, helping researchers capture proteins that specifically bind to the CD20 extracellular domain. This method might help clarify CD20's function in B-cell signaling pathways and reveal new regulatory mechanisms. The yeast expression system appears to provide appropriate eukaryotic protein folding that may be essential for preserving natural protein interactions.
3. ELISA-Based Binding Assays
Researchers can utilize the recombinant protein as a coating antigen in enzyme-linked immunosorbent assays to examine CD20-specific binding interactions. Scientists might investigate binding kinetics and specificity of current anti-CD20 antibodies or analyze sera from immunized animals. The His-tag enables oriented attachment to nickel-coated plates, which could enhance assay consistency and sensitivity. This application seems particularly useful for screening hybridoma supernatants during antibody development projects focused on mouse CD20.
4. Structural and Biochemical Characterization Studies
This purified CD20 fragment can undergo various biophysical analyses to better understand structural properties of the mouse CD20 extracellular domain. Methods like circular dichroism spectroscopy, dynamic light scattering, or analytical ultracentrifugation might provide insights into protein folding, stability, and oligomerization states. The high purity level makes it appropriate for mass spectrometry analysis to verify protein identity and detect post-translational modifications. Such studies could contribute to understanding the molecular foundation of CD20 function in mouse B-cell biology.
-SDS.jpg)
