Cholera toxin

  Cat. No.:  DC42519  
Chemical Structure
9012-63-9
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More than 5000 active chemicals with high quality for research!
Field of application
Cholera toxin (Choleragen), an AB(5)-subunit toxin, enters host cells by binding the ganglioside GM1 at the plasma membrane (PM) and travels retrograde through the trans-Golgi Network into the endoplasmic reticulum (ER). Choleragen activates adenylate cyclase by catalyzing ADP-ribosylation of Gs alpha, the stimulatory guanine nucleotide-binding protein.
Cas No.: 9012-63-9
Synonyms: Cholera toxin
SMILES: [Cholera toxin]
Sotrage: Powder -20°C 3 years 4°C 2 years In solvent -80°C 6 months -20°C 1 month
MSDS
TITLE DOWNLOAD
MSDS_26147_DC42519_9012-63-9
COA
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Cat. No. Product name Field of application
DC46365 TDI-10229 TDI-10229 is a potent and orally bioavailable inhibitor of soluble adenylyl cyclase (sAC, ADCY10). TDI-10229 displays nanomolar inhibition of sAC in both biochemical and cellular assays (IC50 of 195 nM) and exhibits mouse pharmacokinetic properties sufficient to warrant its use as an in vivo tool compound.
DC44789 TIP 39, Tuberoinfundibular Neuropeptide TIP 39, Tuberoinfundibular Neuropeptide is a neuropeptide and parathyroid hormone 2 receptor (PTH2R) agonist. TIP 39 is highly conserved among species. TIP39 from all species activates adenylyl cyclase and elevates intracellular calcium levels through parathyroid hormone 2 receptor (PTH2R).
DC42519 Cholera toxin Cholera toxin (Choleragen), an AB(5)-subunit toxin, enters host cells by binding the ganglioside GM1 at the plasma membrane (PM) and travels retrograde through the trans-Golgi Network into the endoplasmic reticulum (ER). Choleragen activates adenylate cyclase by catalyzing ADP-ribosylation of Gs alpha, the stimulatory guanine nucleotide-binding protein.
DC12017 NKY80 A potent, selective adenylyl cyclase AC5/6 inhibitor with IC50 of 7.7/17 uM, respectively.
DC12016 NB 001 A potent, relatively selective and orally active adenylyl cyclase 1 (AC1) inhibitor with IC50 of 10 uM (cAMP production inhibition).
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