Recombinant Human Galectin-8 (LGALS8) is a full-length protein expressed in E. coli with an N-terminal GST tag. The protein achieves a purity level above 90% as assessed by SDS-PAGE, which appears to provide reliable quality for research applications. Its biological activity has been confirmed through binding capacity in a functional ELISA, where it binds to immobilized SLC31A1 with an EC50 range of 373.90-524.30 μg/ml. This suggests consistent performance in experimental settings.
Galectin-8 belongs to the galectin family, known for binding beta-galactoside sugars. It likely plays important roles in various biological processes, including cell adhesion, migration, and immune response modulation. Galectin-8 appears to be involved in intracellular signaling pathways. Numerous studies have focused on this protein due to its significance in cellular interactions and potential implications in various physiological and pathological 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 with SLC31A1
The demonstrated binding activity between LGALS8 and SLC31A1 in functional ELISA provides a foundation for investigating this protein-protein interaction in detail. Researchers can use this recombinant protein to characterize binding kinetics, determine optimal binding conditions, and map interaction domains through competitive binding assays. The GST tag allows for purification and immobilization strategies that support surface plasmon resonance or other biophysical binding studies. This application could help elucidate the molecular mechanisms underlying LGALS8-SLC31A1 interactions in cellular contexts.
2. GST Pull-Down Assays for Binding Partner Identification
The N-terminal GST tag makes this protein well-suited for GST pull-down experiments to identify novel LGALS8 binding partners from cell lysates or protein libraries. High purity (>90%) appears to ensure minimal background interference in these assays, while the full-length construct (1-317aa) preserves all potential binding domains. Researchers can immobilize the GST-LGALS8 fusion protein on glutathione-sepharose beads and screen for interacting proteins using mass spectrometry or Western blot analysis. This approach may reveal previously unknown components of LGALS8-mediated signaling pathways or regulatory networks.
3. Antibody Development and Validation
This highly pure, full-length recombinant LGALS8 serves as what appears to be an excellent antigen for generating specific antibodies against human galectin-8. The protein can be used to immunize animals for polyclonal antibody production or as a screening antigen for monoclonal antibody development. The recombinant protein also provides a standardized positive control for validating antibody specificity and determining optimal working concentrations in various immunoassays. The GST tag allows for tag-specific detection methods during antibody characterization studies.
4. Functional ELISA Development and Optimization
Given the established activity testing method using SLC31A1 binding, this recombinant protein can serve as a reference standard for developing and optimizing functional ELISA protocols. Researchers can use the known EC50 range (373.90-524.30 μg/ml) as a benchmark for assay sensitivity and reproducibility testing. The protein enables standardization of binding assays across different laboratories. It also supports the development of competitive binding assays to screen for small molecule inhibitors or other galectin-8 ligands.
5. Biochemical Characterization and Structure-Function Studies
The full-length, biologically active recombinant protein provides what appears to be an ideal tool for comprehensive biochemical characterization of LGALS8 properties. Researchers can investigate protein stability under various conditions, determine optimal storage parameters, and analyze structural features through techniques like circular dichroism spectroscopy. The demonstrated binding activity allows for structure-function relationship studies. This includes examining the effects of pH, ionic strength, and temperature on protein-protein interactions, which may contribute to a deeper understanding of galectin-8 biology.
