This recombinant Shigella dysenteriae serotype 1 60KDA chaperonin (groL) comes from an E. coli expression system and spans amino acids 101-548. The protein carries an N-terminal 10xHis-SUMO tag plus a C-terminal Myc tag, making purification and detection straightforward. SDS-PAGE analysis confirms purity levels above 90%, which should provide reliable material for research applications.
Chaperonins such as groL appear to be essential players in how cells fold their proteins properly. They seem to help newly made proteins—or those damaged by stress—find their correct three-dimensional shapes. Without these molecular assistants, cellular protein networks might collapse. Scientists have been studying chaperonins across many biological pathways, though the exact mechanisms behind their function remain an active area of investigation.
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.
Shigella dysenteriae GroL (60 kDa chaperonin) is a complex oligomeric protein that requires precise folding, proper ATPase activity, and specific oligomerization into a functional double-ring tetradecamer structure. The E. coli expression system is homologous for this bacterial chaperonin, which increases the probability of correct domain folding. However, the partial fragment (101-548aa) lacks the critical N-terminal domain (1-100aa) that contains essential structural elements for proper oligomerization and functional activity. The dual N-terminal 10xHis-SUMO tag (∼15 kDa) and C-terminal Myc tag (∼1.2 kDa) may sterically interfere with the protein's oligomerization interfaces and functional domains. While individual domains may fold correctly, the protein cannot form functional oligomers or exhibit authentic chaperonin activity due to the missing N-terminal region and tag interference.
1. Biophysical Characterization
Basic biophysical characterization can be performed, but will not reflect native chaperonin properties. Techniques like circular dichroism spectroscopy can analyze secondary structure content of individual domains, and size-exclusion chromatography can assess aggregation state. However, results will describe a partial, monomeric fragment rather than the functional oligomeric complex, and the large tags will dominate the biophysical properties.
2. Antibody Development and Validation
This application is suitable for generating antibodies against linear epitopes within the 101-548aa region. Antibody development relies on antigenic sequence recognition rather than functional protein conformation. The high purity (>90%) ensures minimal contamination-related issues during immunization protocols. However, antibodies may not efficiently recognize conformational epitopes dependent on full-length oligomerization.
Final Recommendation & Action Plan
This partial GroL fragment (101-548aa) with large dual tags is unsuitable for functional chaperonin studies but can be used for limited applications. The missing N-terminal domain prevents proper oligomerization essential for GroL function. Application 1 (Biophysical Characterization) can provide basic domain-level structural information but will not reflect native chaperonin properties. Application 2 (Antibody Development) is well-suited for generating region-specific antibodies. For reliable GroL research requiring functional activity, use full-length protein (1-548aa) with minimal tags to preserve oligomerization capability.
