Recombinant Human Pro-glucagon (GCG) is produced in E. coli and comes with an N-terminal 6xHis-GST tag. This partial protein covers amino acids 53-89 and appears to be purified to greater than 85% purity based on SDS-PAGE analysis. The product is intended for research use only, though it seems to perform consistently across different experimental setups.
Pro-glucagon acts as a precursor to several key peptides, including glucagon and GLP-1. These peptides play important roles in glucose metabolism and insulin regulation. The derivatives from pro-glucagon are involved in pathways related to energy balance and have become a central focus in metabolic research and diabetes studies.
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. Antibody Development and Validation Studies
This recombinant human pro-glucagon fragment (amino acids 53-89) may work well as an immunogen or screening antigen when developing antibodies that target this particular region of the pro-glucagon precursor protein. The N-terminal 6xHis-GST tag makes purification and immobilization straightforward for ELISA-based antibody screening. Scientists can likely use this protein to create monoclonal or polyclonal antibodies that recognize this specific portion of pro-glucagon. Such antibodies might prove valuable for detecting processing intermediates or investigating pro-glucagon biology more broadly. The high purity (>85%) should help maintain consistent results during immunization and screening work.
2. Protein-Protein Interaction Studies
The GST tag allows for pull-down assays that could identify potential binding partners interacting with this particular region of human pro-glucagon. Scientists can attach the GST-tagged protein to glutathione-sepharose beads and mix it with cell lysates or purified protein libraries to capture any interacting molecules. This method might uncover previously unknown regulatory proteins, processing enzymes, or chaperones that specifically bind to amino acids 53-89 of pro-glucagon. The 6xHis tag offers another purification and detection route for these interaction experiments.
3. Biochemical Characterization and Structural Studies
This well-defined pro-glucagon fragment appears suitable for detailed biochemical analysis. Techniques like circular dichroism spectroscopy and dynamic light scattering could help characterize its structural properties. The purified protein lets researchers examine folding behavior, stability, and conformational shifts within this specific region under different buffer conditions and temperatures. These studies may provide clues about how this portion of pro-glucagon influences the overall structure and processing of the complete precursor protein.
4. Enzyme Substrate Studies
The recombinant pro-glucagon fragment can likely function as a substrate for studying prohormone convertases and other proteolytic enzymes that break down glucagon. Scientists might use this protein in laboratory cleavage assays to map specific cutting sites within the 53-89 amino acid region and calculate kinetic parameters for different processing enzymes. The tags make detection and measurement of cleavage products relatively simple through Western blotting or other tag-specific detection approaches.
