Vibrio cholerae serotype O1 CTXB Protein (HEK293, His)

The pentameric ring of the B subunit of the CTXB protein guides the A subunit by binding to GM1 ganglioside on intestinal epithelial cells. This loop binds five GM1 gangliosides and promotes the specific interaction of the toxin with its cellular receptor. Vibrio cholerae serotype O1 CTXB Protein (HEK293, His) is the recombinant virus-derived Vibrio cholerae serotype O1 CTXB protein, expressed by HEK293, with C-His labeled tag.

The CTXB protein, represented by its B subunit pentameric ring, plays a pivotal role in guiding the A subunit to its target by binding to GM1 gangliosides on the surface of intestinal epithelial cells. The pentameric ring is adept at binding five GM1 gangliosides, facilitating the specific interaction between the toxin and its cellular receptor. Notably, the CTXB B subunit lacks toxic activity on its own. The holotoxin, known as choleragen, comprises a pentameric ring of B subunits, forming a structure with a central pore occupied by the A subunit. The A subunit itself consists of two chains, A1 and A2, connected by a disulfide bridge, further emphasizing the intricate architecture and functionality of this toxin.

Virus

HEK293

C-His

P01556 (T22-N124)

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Full Length of Mature Protein

Approximately 16-17 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder.

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

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.