SML0655
Shiga toxin 1, B subunit, HIS-tagged
recombinant, expressed in E. coli, ≥95% (SDS-PAGE)
Synonym(s):
SLT1, STX1, STxB
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.77
Recommended Products
recombinant
expressed in E. coli
Quality Level
assay
≥95% (SDS-PAGE)
form
lyophilized
suitability
endotoxin tested
shipped in
dry ice
storage temp.
−20°C
Biochem/physiol Actions
The Shiga toxins are a family of related protein toxins secreted by certain types of bacteria.
The Shiga toxins are a family of related protein toxins secreted by certain types of bacteria. Shiga toxin (Stx) is produced by Shigella dysenteriae; whereas, the Shiga-like toxins, Stx1 and Stx2, with a few known isoforms, are secreted by specific strains of Escherichia coli named Shiga-toxin-producing E. coli (STEC), such as E. coli O157:H7, which causes bloody diarrhea and hemorrhagic colitis in humans, sometimes resulting in fatal systemic complications.
Stx1 is identical to Stx, while the Stx2 isoforms share less sequence similarity with Stx (∼60%) and are immunologically distinct. In spite of the differences in their amino acid sequence, all Stx isoforms share the same overall toxin structure and mechanism of action.
Shiga toxins consists of two polypeptides. An A chain and a B chain non-covalently associate with an apparent stoichiometry of one A and five B chains to form the holotoxin. The catalytic A subunit has
RNA N-glycosidase activity that inhibits eukaryotic protein synthesis. The B subunits form a pentamer, which recognizes and binds to the functional cell-surface receptor globotriaosylceramide [Gb3; Gala(1-4)-Galb(1-4)-Glcb1-ceramide]. Gb3 is overexpressed in membranes of numerous tumor cells, therefore STxB binding to Gb3 receptors may be useful for cell-specific vectorization, labeling, and imaging purposes.
Stx1 is identical to Stx, while the Stx2 isoforms share less sequence similarity with Stx (∼60%) and are immunologically distinct. In spite of the differences in their amino acid sequence, all Stx isoforms share the same overall toxin structure and mechanism of action.
Shiga toxins consists of two polypeptides. An A chain and a B chain non-covalently associate with an apparent stoichiometry of one A and five B chains to form the holotoxin. The catalytic A subunit has
RNA N-glycosidase activity that inhibits eukaryotic protein synthesis. The B subunits form a pentamer, which recognizes and binds to the functional cell-surface receptor globotriaosylceramide [Gb3; Gala(1-4)-Galb(1-4)-Glcb1-ceramide]. Gb3 is overexpressed in membranes of numerous tumor cells, therefore STxB binding to Gb3 receptors may be useful for cell-specific vectorization, labeling, and imaging purposes.
Physical form
The product is a recombinant Shiga toxin B subunit, which contains 69 amino acid residues and a HIS-tag at the C-terminus. It is lyophilized from 0.2 μm filtered solution of phosphate buffer without any carrier protein.
Preparation Note
Reconstitute the contents of the vial using water to a concentration of 0.1-1.0 mg/mL. This solution can then be diluted into other aqueous buffers and stored at 2-8 °C for up to 4 months or at -20 °C for extended use.
Analysis Note
Gb3 Binding activity: significant binding above background is achieved with ≤1 μg/mL of STxB. The activity of STxB is measured by its ability to bind to Gb3, which requires its pentameric form.[1]
signalword
Warning
hcodes
pcodes
Hazard Classifications
Acute Tox. 4 Dermal - Acute Tox. 4 Inhalation - Acute Tox. 4 Oral
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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In-Sun Shin et al.
Chemical & pharmaceutical bulletin, 54(4), 522-527 (2006-04-06)
A two-step binding assay for globotriaosylceramide (Gb3) content was developed by histidine-tagging strategy, which is a well-established method for the purification of recombinant proteins. The complete binding of the recombinant His-tagged Shiga toxin 1B subunit (1B-His) (1 microg/ml) to the
Xihua Yue et al.
BMC biology, 19(1), 194-194 (2021-09-09)
KDEL receptor helps establish cellular equilibrium in the early secretory pathway by recycling leaked ER-chaperones to the ER during secretion of newly synthesized proteins. Studies have also shown that KDEL receptor may function as a signaling protein that orchestrates membrane
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