The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use at an assay dependent dilution. Predicted molecular weight: 14, 29 kDa.
Use at an assay dependent dilution.
The holotoxin (choleragen) consists of a pentameric ring of B subunits whose central pore is occupied by the A subunit. The A subunit contains two chains, A1 and A2, linked by a disulfide bridge. The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself.
After binding to gangliosides GM1 in lipid rafts, through the subunit B pentamer, the holotoxin and the gangliosides are internalized. The holotoxin remains bound to GM1 until arrival in the ER. The A subunit has previously been cleaved in the intestinal lumen but the A1 and A2 chains have remained associated. In the ER, the A subunit disulfide bridge is reduced, the A1 chain is unfolded by the PDI and disassembled from the rest of the toxin. Then, the membrane-associated ER oxidase ERO1 oxidizes PDI, which releases the unfolded A1 chain. The next step is the retrotranslocation of A1 into the cytosol. This might be mediated by the protein-conducting pore SEC61. Upon arrival in the cytosol, A1 refolds and avoids proteasome degradation. In one way or another, A1 finally reaches its target and induces toxicity.
Cholera enterotoxin B chain antibody
Cholera enterotoxin gamma chain antibody
Cholera enterotoxin subunit A antibody
Cholera enterotoxin subunit B antibody
Anti-Cholera Toxin antibody 图像
Western blot - Anti-Cholera Toxin antibody (ab123129)
Anti-Cholera Toxin antibody (ab123129) at 1/2000 dilution + Culture medium of Vibrio cholerae 569B strain
Predicted band size : 14, 29 kDa
SDS-PAGE - Anti-Cholera Toxin antibody (ab123129)
Culture medium of Vibrio cholerae 569B strain subjected to electrophoresis under reducing condition followed by silver-staining.