Recombinant Rat Sortilin (Sort1) is expressed in E.coli and consists of the 610-754 amino acid region with an N-terminal 6xHis-tag for convenient purification and detection. The protein is provided at a purity level greater than 90%, confirmed by SDS-PAGE analysis, ensuring high quality for research applications. It is intended for research use only and does not contain endotoxin specifications.
Sortilin appears to be a central player in cellular trafficking and signaling, functioning as a receptor that likely influences how various proteins get sorted within cells. The protein seems involved in pathways related to lipid metabolism and neurodegenerative processes. As a multifunctional receptor, studying Sortilin may be crucial for understanding mechanisms in cellular communication and disease-related 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. Protein-Protein Interaction Studies Using Pull-Down Assays
The N-terminal 6xHis-tagged recombinant rat sortilin fragment (610-754aa) can be immobilized on nickel-affinity resins to identify potential binding partners from rat tissue lysates or cell extracts. This C-terminal region of sortilin might contain important protein interaction domains that could be systematically studied through pull-down experiments followed by mass spectrometry analysis. The high purity (>90%) ensures minimal background binding from contaminating proteins during interaction studies. This approach would help researchers piece together the molecular networks involving sortilin in rat cellular systems.
2. Antibody Development and Validation
This purified recombinant protein fragment works well as an immunogen for generating polyclonal or monoclonal antibodies specific to the 610-754aa region of rat sortilin. The high purity and defined sequence boundaries make it suitable for immunization protocols and subsequent antibody characterization. Generated antibodies can be validated for specificity using ELISA, Western blot, and immunoprecipitation assays with the same recombinant protein as a positive control. Such antibodies would likely become valuable research tools for studying sortilin expression and localization in rat tissues and cell lines.
3. Structural and Biophysical Characterization Studies
The recombinant sortilin fragment can be used for detailed structural analysis through techniques such as circular dichroism spectroscopy, dynamic light scattering, and analytical ultracentrifugation to determine its folding state and oligomerization properties. Nuclear magnetic resonance or X-ray crystallography studies might provide atomic-level structural information about this specific C-terminal region of rat sortilin. The 6xHis tag makes protein purification straightforward for these biophysical studies while the high purity ensures reliable spectroscopic measurements. These studies would contribute to understanding the structure-function relationships within the sortilin protein family.
4. Comparative Species Analysis and Evolutionary Studies
This rat sortilin fragment can be used alongside corresponding recombinant fragments from other species to conduct comparative binding studies and evolutionary analysis of sortilin function. Cross-species interaction assays using this defined 610-754aa region would help identify conserved functional domains and species-specific binding preferences. The standardized expression system and purification approach allows for direct comparison with orthologous proteins from mouse, human, or other mammalian species. Such comparative studies may provide insights into the evolutionary conservation of sortilin's molecular functions across different mammalian lineages.
