Recombinant Rat Galectin-4 (Lgals4) is produced in an E.coli expression system, containing amino acids 1-324 to create the full-length protein. The product comes tag-free, which appears to preserve its native form, and shows a purity level greater than 85% as confirmed by SDS-PAGE analysis. It's designed for research use only, with what seems to be a focus on precision and quality for various experimental applications.
Galectin-4 is a carbohydrate-binding protein that likely plays a significant role in cell-cell and cell-matrix interactions. Research suggests it's involved in several biological processes, including modulation of immune responses and regulation of cell growth and apoptosis. As a member of the galectin family, this protein may be crucial in research aimed at understanding its function in cellular communication and 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.
1. Carbohydrate-Binding Specificity Studies
This recombinant rat galectin-4 works well in glycan array experiments and surface plasmon resonance assays to characterize its carbohydrate-binding specificity and affinity. Scientists can examine how the protein interacts with various β-galactoside-containing oligosaccharides and glycoconjugates to map out its binding preferences. The tag-free design is particularly valuable here - it means binding studies should reflect the native protein's carbohydrate recognition properties without potential interference from affinity tags. These types of studies appear essential for understanding the molecular basis of galectin-4's biological functions and its role in glycobiology research.
2. Antibody Development and Validation
The full-length recombinant rat galectin-4 works as an ideal antigen for generating specific antibodies against this protein. Scientists can use this purified protein to immunize animals for polyclonal antibody production or as a screening antigen for monoclonal antibody development. The high purity level (>85%) likely ensures consistent and reliable immunization results. The recombinant protein can also validate antibody specificity through ELISA, Western blot, and other immunoassays in galectin-4 research applications.
3. Protein-Protein Interaction Studies
This recombinant galectin-4 proves useful in pull-down assays and co-immunoprecipitation experiments to identify and characterize protein binding partners. Scientists can attach the galectin-4 protein to appropriate matrices to capture interacting proteins from cell lysates or tissue extracts. The tag-free format offers a clear advantage here - it eliminates potential artifacts that might arise from tag-mediated interactions. Such experiments may help clarify the protein networks and signaling pathways involving galectin-4 in various biological processes.
4. Structural and Biophysical Characterization
The purified recombinant rat galectin-4 can support detailed structural studies including X-ray crystallography, NMR spectroscopy, and cryo-electron microscopy experiments. Scientists can investigate the protein's three-dimensional structure, conformational dynamics, and structural changes upon ligand binding. The high purity and tag-free nature appear to make this protein well-suited for biophysical techniques such as dynamic light scattering, analytical ultracentrifugation, and thermal stability assays. These studies provide fundamental insights into the structure-function relationships of galectin-4.
5. Cell-Based Functional Assays
This recombinant galectin-4 can be applied in various cell culture experiments to study its effects on cellular processes such as adhesion, migration, and apoptosis. Scientists can treat cultured cells with the purified protein to investigate dose-dependent responses and examine downstream signaling pathways. The protein also works in cell binding assays to study galectin-4's interaction with cell surface glycoproteins and glycolipids. Such experiments help scientists understand the extracellular functions of galectin-4 in cellular biology and tissue homeostasis.
