Cholera Toxin Beta Antibody [FITC]

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Product Details

Summary
Reactivity BaSpecies Glossary
Applications ELISA, IP
Clonality
Polyclonal
Host
Rabbit
Conjugate
FITC

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Cholera Toxin Beta Antibody [FITC] Summary

Immunogen
Purified choleragenoid
Specificity
NB100-63067 is specific for the beta subunit of cholera toxin. The beta subunit of cholera toxin binds to a GM1-ganglioside receptor which is widely accepted to initiate toxin action by triggering uptake and delivery of the toxin alpha subunit into cells. The holotoxin consists of a pentameric ring of beta subunits whose central pore is occupied by the alpha subunit. The alpha subunit contains two chains, A1 and A2, linked by a disulfide bridge. The alpha subunit (and cholera toxin) activate the adenylate cyclase enzyme in cells of the intestinal mucosa leading to increased levels of intracellular cAMP. This antibody immunoprecipitates cholera toxin in gel techniques.
Isotype
IgG
Clonality
Polyclonal
Host
Rabbit
Purity
IgG purified
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Applications/Dilutions

Dilutions
  • ELISA 1:100-1:2000
  • Immunoprecipitation 1:10-1:500

Packaging, Storage & Formulations

Storage
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
Buffer
PBS and 1.0% BSA
Preservative
0.05% Sodium Azide
Purity
IgG purified

Alternate Names for Cholera Toxin Beta Antibody [FITC]

  • Cholera enterotoxin B chain
  • Cholera enterotoxin beta chain
  • Cholera enterotoxin gamma chain
  • Cholera enterotoxin subunit B
  • Cholera toxin B protein
  • Choleragenoid
  • CTX B
  • CTXB
  • TOX B
  • toxB
  • VC1456

Background

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. The beta subunit of cholera toxin binds to a GM1-ganglioside receptor which is widely accepted to initiate toxin action by triggering uptake and delivery of the toxin alpha subunit into cells. The holotoxin consists of a pentameric ring of beta subunits whose central pore is occupied by the alpha subunit. The alpha subunit contains two chains, A1 and A2, linked by a disulfide bridge. The alpha subunit (and cholera toxin) activate the adenylate cyclase enzyme in cells of the intestinal mucosa leading to increased levels of intracellular cAMP.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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