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Cat. No.: RMLIF-10 (for 10μg)

Cat. No.: RMLIF-50 (for 50μg)

Cat. No.: RMLIF-200 (for 200μg)

 

Synonyms    

CTB; Choleragen; CTX; Ctx; CT


Purity    

>98% by SDS-PAGE and HPLC analyses.


Biological Activity    

Data Not Available.


Physical Appearance    

Sterile colorless liquid.


Formulation    

Supplied as a 0.2µM filtered solution in 5mM PB, pH7.0, 75mM NaCl, with 50% glycerol.


Endotoxin    

Less than 0.1EU/µg of rCTB as determined by LAL method.


Reconstitution    

－


Category    

Others


Background    

Cholera toxin is protein complex secreted by the bacterium Vibrio cholerae. CTX is responsible for the massive, watery diarrhea characteristic of cholera infection. The cholera toxin is an oligomeric complex made up of six protein subunits: a single copy of the A subunit (part A, enzymatic), and five copies of the B subunit (part B, receptor binding), denoted as AB5. Subunit B binds while subunit A activates the G protein which activates adenylate cyclase. The five B subunits - each weighing 11 kDa, form a five-membered ring. The A subunit which is 28 kDa, has two important segments. The A1 portion of the chain (CTA1) is a globular enzyme payload that ADP-ribosylates G proteins, while the A2 chain (CTA2) forms an extended alpha helix which sits snugly in the central pore of the B subunit ring. This structure is similar in shape, mechanism, and sequence to the heat-labile enterotoxin secreted by some strains of the Escherichia coli bacterium.


Amino Acid Sequence    

TPQNITDLCA EYHNTQIYTL NDKIFSYTES LAGKREMAII TFKNGAIFQV EVPGSQHIDS QKKAIERMKD TLRIAYLTEA KVEKLCVWNN KTPHAIAAIS MAN

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