产品名称
Cholera Toxin B subunit, ≥95% (SDS-PAGE), lyophilized powder
SMILES string
CCOc1ccccc1C(=O)Nc2ccc(Cl)c(c2)C(F)(F)F
InChI
1S/C16H13ClF3NO2/c1-2-23-14-6-4-3-5-11(14)15(22)21-10-7-8-13(17)12(9-10)16(18,19)20/h3-9H,2H2,1H3,(H,21,22)
InChI key
YDXZSNHARVUYNM-UHFFFAOYSA-N
assay
≥95% (SDS-PAGE)
form
lyophilized powder
mol wt
~12 kDa
composition
Protein, ~5% Lowry
impurities
≤0.5% Cholera toxin A subunit (SDS-PAGE)
solubility
H2O: 10 mg/mL
storage temp.
2-8°C
Quality Level
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General description
Cholera Toxin is a heterohexameric AB5 enterotoxin. Cholera Toxin B subunit is the the B subunit pentamer of cholera toxin produced by Vibrio cholera. It is generally involved in the cell trafficking and signalling machineries.
Application
Cholera Toxin B subunit has been used:
- for macrophage stimulation and i.p. injection in a study to determine the endotoxin sensitivity of Caspase-4.
- in transganglionic and retrograde tract-tracing method combined with dual-immunofluorescence histochemistry of adult rat Vmes neuron cells.
Biochem/physiol Actions
The cholera toxin B subunit is used for track tracing in neurological research, taking advantage of GM1 ganglioside binding and retrograde transport.
The cholera toxin B subunit is used for track tracing in neurological research, taking advantage of GM1 ganglioside binding and retrograde transport. Tissue culture cells treated with cholera toxin are not killed and tissues of animals do not become necrotic.
Features and Benefits
This compound is a featured product for Cyclic Nucleotide research. Click here to discover more featured Cyclic Nucleotide products. Learn more about bioactive small molecules for other areas of research at sigma.com/discover-bsm.
Packaging
Package size based on protein content
Physical form
Lyophilized powder containing Tris buffer salts, sodium chloride, sodium azide, and sodium EDTA.
Preparation Note
When reconstituted with water to a final concentration of 1 mg of CTB per ml, the solution will contain 0.05 M Tris buffer, pH 7.5, 0.2 M NaCl, 3 mM NaN3 and 1 mM sodium EDTA.
Analysis Note
Activity measured by ELISA using ganglioside GM1-coated multiwell plates, rabbit anti-Cholera toxin B subunit antibodies, and peroxidase-labeled goat anti-rabbit IgG as the secondary antibody. 50% saturation of binding was achieved with 0.05-1 μg of Cholera toxin B subunit per mL.
signalword
Warning
hcodes
Hazard Classifications
Acute Tox. 4 Dermal - Acute Tox. 4 Inhalation - Aquatic Chronic 3
存储类别
11 - Combustible Solids
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
Lolke De Haan et al.
Molecular membrane biology, 21(2), 77-92 (2004-06-19)
Cholera toxin (Ctx) from Vibrio cholerae and its closely related homologue, heat-labile enterotoxin (Etx) from Escherichia coli have become superb tools for illuminating pathways of cellular trafficking and immune cell function. These bacterial protein toxins should be viewed as conglomerates
R G Zhang et al.
Journal of molecular biology, 251(4), 550-562 (1995-08-25)
Cholera toxin, a heterohexameric AB5 enterotoxin released by Vibrio cholera, induces a profuse secretory diarrhea in susceptible hosts. Choleragenoid, the B subunit pentamer of cholera toxin, directs the enzymatic A subunit to its target by binding the GM1 gangliosides exposed
Jung Won Youm et al.
FEBS letters, 579(30), 6737-6744 (2005-11-29)
Beta amyloid (Abeta) is believed one of the major pathogens of Alzheimer's disease (AD), and the reduction of Abeta is considered a primary therapeutic target. Immunization with Abeta can reduce Abeta burden and pathological features in transgenic AD model mice.
Stefan Achtsnicht et al.
PloS one, 14(7), e0219356-e0219356 (2019-07-06)
Cholera is a life-threatening disease caused by the cholera toxin (CT) as produced by some Vibrio cholerae serogroups. In this research we present a method which directly detects the toxin's B subunit (CTB) in drinking water. For this purpose we
Shun-Nan Ge et al.
The Journal of comparative neurology, 518(15), 3149-3168 (2010-06-10)
VGLUT1 and VGLUT2 have been reported to show complementary distributions in most brain regions and have been assumed to define distinct functional elements. In the present study, we first investigated the expression of VGLUT1 and VGLUT2 in the trigeminal sensory
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