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.
Rat Sort1 is a transmembrane receptor protein that requires precise folding, proper domain organization (including a VPS10p domain and transmembrane region), and specific oligomerization for its functional activity in protein sorting and trafficking. The E. coli expression system cannot provide the eukaryotic folding environment, membrane integration, or post-translational modifications (such as glycosylation) required for this complex receptor. The partial fragment (610-754aa) represents only the C-terminal region and lacks critical N-terminal domains (including the ligand-binding VPS10p domain) essential for full functionality. The N-terminal 6xHis-tag may sterically interfere with the protein's structural domains. While the protein may be soluble, the probability of correct folding with functional receptor activity is extremely low.
1. Antibody Development and Validation
This application is highly suitable as antibody development relies on antigenic sequence recognition rather than functional protein folding. The partial fragment provides specific epitopes within the 610-754aa region for generating antibodies against rat sortilin. The high purity (>90%) ensures minimal contamination-related issues during immunization protocols.
2. Structural and Biophysical Characterization Studies
These studies are essential for determining folding status, but will not reflect native sortilin structure. Techniques should include circular dichroism spectroscopy to assess secondary structure, size-exclusion chromatography to evaluate oligomeric state, and thermal stability assays. However, results will describe a misfolded fragment rather than the full-length, membrane-integrated receptor.
Final Recommendation & Action Plan
This partial sortilin fragment (610-754aa) expressed in E. coli is fundamentally unsuitable for functional studies due to the essential requirements for membrane integration and complete domain organization that cannot be met. The protein cannot be used for interaction studies and comparative analysis. Application 2 (structural characterization) provides only basic physical characterization of the fragment itself. Application 1 (antibody development) can proceed immediately. For reliable sortilin research, use a full-length protein expressed in mammalian systems that supports proper membrane integration, glycosylation, and preserves native conformational epitopes and ligand-binding capability.
