protein

CTXB Protein, Vibrio cholerae

HY-P71064

10 μg;50 μg

170;510 USD

CTXB Protein, Vibrio cholerae

proteins

E. coli

10 μg;50 μg

170;510 USD

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.

Others

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.

Cholera enterotoxin subunit B; Cholera enterotoxin B chain; Cholera enterotoxin gamma chain; Choleragenoid; ctxB; toxB

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

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

Room temperature in continental US;may vary elsewhere.