Recombinant Human Neuropeptide B (NPB) is produced in E. coli and comprises the full length of the mature protein spanning amino acids 25-53. This product carries an N-terminal GST tag, which aids in protein purification and detection. SDS-PAGE analysis shows purity greater than 90%, making it a high-quality protein that appears well-suited for research purposes. This product is intended for research use only and not for human therapeutic or diagnostic applications.
Neuropeptide B (NPB) is a neuropeptide that seems to play important roles in various signaling pathways within the central nervous system. It likely helps modulate neuroendocrine functions and has been linked to processes such as feeding behavior and energy homeostasis. NPB has become a target of interest in neurological research due to its potential impact on behavior and physiological regulation.
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.
Human NPB is a small neuropeptide that requires precise folding, proper tertiary structure, and specific conformational epitopes for its functional activity in receptor binding and signaling. The E. coli expression system cannot provide the eukaryotic folding environment necessary for this neuropeptide's correct conformation. The large N-terminal GST tag (∼26 kDa) is massively larger than the NPB peptide itself (29 aa, ∼3 kDa), creating severe steric interference that will completely disrupt the peptide's receptor-binding interfaces and functional domains. The probability of correct folding with functional bioactivity is essentially zero.
1. Antibody Development and Validation
This application has severe limitations. While antibodies can be generated, the immune response will primarily target the large foreign GST tag rather than the small NPB peptide. Antibodies may not recognize the native, properly folded neuropeptide in its physiological context.
2. Biochemical Characterization and Structural Studies
Basic biophysical analysis can be performed, but will not reflect native NPB structure. The GST tag will dominate all physical properties, and results will describe an artificial construct rather than the physiological neuropeptide.
Final Recommendation & Action Plan
This GST-tagged NPB construct expressed in E. coli is fundamentally unsuitable for functional neuropeptide research due to the extreme size disparity between the tag (26 kDa) and the peptide (3 kDa). The GST tag is nearly nine times larger than NPB itself, making all functional studies biologically irrelevant. Applications 1 and 2 have severe limitations and will not provide insights into native NPB biology. For reliable NPB research, use synthetic peptides or mammalian-expressed neuropeptides that preserve native conformation and receptor-binding capability.
