CTXB Protein, Vibrio cholerae

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. CTXB Protein, Vibrio cholerae is the recombinant CTXB protein, expressed by E. coli , with tag free. The total length of CTXB Protein, Vibrio cholerae is 103 a.a., with molecular weight of ~11.0 kDa.

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.

Others

E. coli

Tag Free

P01556 (T22-N124)

57740119

TPQNITDLCAEYHNTQIYTLNDKIFSYTESLAGKREMAIITFKNGAIFQVEVPGSQHIDSQKKAIERMKDTLRIAYLTEAKVEKLCVWNNKTPHAIAAISMAN

Approximately 11.0 kDa

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

Lyophilized powder.

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris-HCl, 200 mM NaCl, pH8.0.

<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. 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.