Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) Cholera enterotoxin subunit B Protein, His Tag (MALS verified)

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GHB-V52H3-50ug
$465.00
GHB-V52H3-500ug
$2,885.00
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GHB-V52H3
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Synonyms

Cholera enterotoxin subunit B/CTxB (Vibrio cholerae)

Source

Vibrio cholerae serotype O1 Cholera enterotoxin subunit B, His Tag (GHB-V52H3) is expressed from human 293 cells (HEK293). It contains AA Thr 22 - Asn 124 (Accession # P01556).

Predicted N-terminus: Thr 22

Molecular Characterization

This protein carries a polyhistidine tag at the C-terminus.

The protein has a calculated MW of 13.5 kDa. The protein migrates as 16-17 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

The protein is designed as a pentamer.

Endotoxin

Less than 1.0 EU per μg by the LAL method / rFC method.

Purity

>95% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

Contact us for customized product form or formulation.

Reconstitution

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

Shipping and Storage

This product is shipped at ambient temperature.

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • -20°C to -70°C for 12 months in lyophilized state;
  • -70°C for 3 months under sterile conditions after reconstitution.

Introduction de fond

Cholera toxin is protein complex secreted by the bacterium Vibrio cholerae. It is responsible for the massive, watery diarrhea characteristic of cholera infection. The B subunit of cholera toxin (CtxB) binds to a GM1-ganglioside receptor, a ubiquitous glycolipid cell surface receptor. This binding is widely accepted to initiate toxin action by triggering uptake and delivery of the toxin A subunit into cells. The beta chain has no toxic activity by itself. The holotoxin 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.