Recombinant Cholera Toxin Beta Protein


SDS-Page: Recombinant Bacterial Cholera Toxin Beta Protein [NBP2-61449] - Recombinant Bacteria, Bacterial Cholera Toxin Beta Protein [NBP2-61449] - Recombinant Bacteria, Viral Cholera Toxin Beta Protein [NBP2-61449] - more

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Recombinant Cholera Toxin Beta Protein Summary

A single non-glycosylated polypeptide chain containing 103 amino acids corresponding to Cholera Toxin Beta Source: E. coli

Uniprot ID: P01556


E. coli
Protein/Peptide Type
Recombinant Protein
>98%, by SDS-PAGE and HPLC
Endotoxin Note
Less than 0.1 EU/ug of Cholera Toxin Beta as determined by LAL method.


  • SDS-Page
Theoretical MW
11.6 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Read Publications using
NBP2-61449 in the following applications:

Packaging, Storage & Formulations

Store at -20C. Avoid freeze-thaw cycles.
0.2 um filtered solution in 5 mM PB, pH 7.0, 75 mM NaCl.
50% glycerol
>98%, by SDS-PAGE and HPLC

Alternate Names for Recombinant Cholera Toxin Beta Protein

  • 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


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.


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

Publications for Cholera Toxin Beta Recombinant Protein (NBP2-61449)(3)

We have publications tested in 1 confirmed species: Bacteria.

We have publications tested in 2 applications: In vitro, LIM.

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In vitro
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Showing Publications 1 - 3 of 3.
Publications using NBP2-61449 Applications Species
Samuel RM, Navickas A, Maynard A et al. Generation of Schwann cell derived melanocytes from hPSCs identifies pro-metastatic factors in melanoma bioRxiv : the preprint server for biology 2023-03-07 [PMID: 36945537] (In vitro) In vitro
Miteva D, Solak A, Dyankova S et al. Assessment of allergenicity of irradiated dairyproducts in a Balb/c mice model Pharmacia 2020-05-03 (LIM, Bacteria)

Vibrio cholerae
LIM Bacteria
Han C, Kang H, Yi J et al. Single-vesicle imaging and co-localization analysis for tetraspanin profiling of individual extracellular vesicles Extracell Vesicles 2021-01-10 [PMID: 33456726]

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