Recombinant Human Pro-glucagon (GCG) is produced in a yeast expression system and contains the amino acid region 53-89. This partial protein includes an N-terminal 6xHis tag, which helps with purification and detection. The product achieves a purity level greater than 90%, as confirmed by SDS-PAGE analysis. Intended for research use only, this recombinant protein offers a reliable tool for various scientific applications.
Pro-glucagon serves as a precursor protein in the production of several hormones, including glucagon and GLP-1, which play key roles in glucose metabolism and homeostasis. This protein appears vital in research focusing on energy balance, diabetes, and metabolic disorders, since it participates in pathways that regulate these physiological processes. Understanding pro-glucagon's role may be crucial for advancing studies in endocrinology and metabolic 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. Antibody Development and Validation Studies
This recombinant human pro-glucagon fragment (amino acids 53-89) can work as an immunogen or antigen for developing specific antibodies against this region of the pro-glucagon precursor protein. The high purity (>90%) and N-terminal 6xHis tag make it suitable for immunization protocols and subsequent antibody screening assays. Researchers can apply this protein in ELISA-based assays to validate antibody specificity and determine binding affinities. The defined amino acid sequence region allows for precise epitope mapping studies to identify specific binding sites within this pro-glucagon segment.
2. Protein-Protein Interaction Studies
The 6xHis-tagged pro-glucagon fragment can work in pull-down assays to identify potential binding partners or regulatory proteins that interact with this specific region of pro-glucagon. The histidine tag enables easy immobilization on nickel-based affinity matrices for capturing interacting proteins from cell lysates or purified protein preparations. This approach may help clarify the molecular mechanisms involved in pro-glucagon processing and regulation. Surface plasmon resonance or other biophysical techniques can also use this purified fragment to characterize binding kinetics with known or suspected interaction partners.
3. Structural and Biophysical Characterization
This purified pro-glucagon fragment provides material for detailed structural studies using techniques such as NMR spectroscopy, circular dichroism, or X-ray crystallography. High purity levels ensure reliable biophysical measurements for determining secondary structure content, thermal stability, and folding characteristics of this specific pro-glucagon region. Researchers can investigate how this segment adopts its native conformation and study the effects of various buffer conditions, pH, or ionic strength on protein stability. The defined amino acid boundaries (53-89) allow for comparative studies with other pro-glucagon fragments or related peptide hormones.
4. Enzyme Substrate Studies for Prohormone Convertases
This pro-glucagon fragment can function as a substrate for in vitro enzymatic studies with prohormone convertases and other proteolytic enzymes involved in peptide hormone processing. Researchers can investigate cleavage specificity, kinetic parameters, and optimal reaction conditions using this defined substrate. The 6xHis tag makes purification and quantification of both substrate and cleavage products straightforward using standard chromatographic methods. Such studies contribute to understanding the biochemical pathways involved in glucagon and GLP-1 maturation from the pro-glucagon precursor.
