Protein is >95% pure as determined by 10% PAGE (coomassie staining).
Purified by affinity chromatographic technique.
Shiga-like toxins (SLTs), also known as verotoxins, are a family of related protein toxins produced by certain strains of bacteria, notably Shigella dysenteriae and Shiga-toxin-producing Escherichia coli (STEC) such as E. coli O157:H7. These toxins are responsible for causing severe gastrointestinal diseases, including bloody diarrhea and hemorrhagic colitis, which can sometimes lead to fatal systemic complications .
Shiga-like toxins consist of two main components: the A subunit and the B subunit. The A subunit has RNA N-glycosidase activity, which inhibits eukaryotic protein synthesis, leading to cell death. The B subunit, on the other hand, forms a pentamer that binds to the functional cell-surface receptor globotriaosylceramide (Gb3). This binding is crucial for the toxin’s entry into the host cell .
The recombinant B subunit of Shiga-like Toxin-1 (SLT-1B) is a 7 kDa protein containing 69 amino acid residues. It is expressed in Escherichia coli and is used in various research applications due to its ability to bind specifically to Gb3 receptors. This specificity makes it a valuable tool for studying cell-specific vectorization, labeling, and imaging purposes .
The recombinant SLT-1B subunit has been utilized in several scientific studies and applications: