form
lyophilized powder
specific activity
~100,000 units/mg protein (HPLC)
mol wt
1,972 Da
solubility
aqueous buffer: ≥5 mg/mL (More soluble under acidic conditions)
storage temp.
−20°C
Biochem/physiol Actions
STa has a tertiary structure, maintained by disulfide bridges, which is required for receptor binding and biological activity. Its receptors are membrane-bound guanylyl cyclases. These receptors are located on enterocytes, colonocytes, and various extraintestinal tissues. STa causes diarrhea in humans by binding to its receptor, stimulating the guanylyl cyclase, and triggering production of cyclic GMP. Endogenous ligands for the STa receptor include guanylin, extracted from intestine, and uroguanylin from urine. These peptides may have a role in the regulation of fluid and electrolytes. Protein kinase C (PKC) phosphorylates and activates the STa receptor/guanylyl cyclase in vitro and in vivo. As a result, stimulators of PKC synergistically enhance STa effects on cGMP and secretion.
Other Notes
E. coli STa is a heat-stable peptide toxin.
One unit is the amount of toxin which produces an intestinal weight/carcass weight ratio of ≥0.083 in 3-day-old mice.
存储类别
6.1A - Combustible acute toxic Cat. 1 and 2 / very toxic hazardous materials
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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相关内容
Product Information Sheet
R N Greenberg et al.
Journal of investigative medicine : the official publication of the American Federation for Clinical Research, 45(5), 276-282 (1997-06-01)
Uroguanylin and guanylin are intestinal peptides that activate a receptor-guanylate cyclase, which is also a receptor for Escherichia coli heat-stable enterotoxin (STa). These peptides may have a role in the body's regulation of fluid and electrolytes. STa, bioactive guanylin, and
R A Giannella
The Journal of laboratory and clinical medicine, 125(2), 173-181 (1995-02-01)
STa represents a family of homologous heat-stable peptide toxins that are elaborated by a variety of bacteria capable of causing enteric disease in human beings. All these peptides have a tertiary structure, maintained by disulfide bridges, which is required for
J K Crane et al.
Molecular and cellular biochemistry, 165(2), 111-120 (1996-12-20)
The heat-stable enterotoxin STa of E. coli causes diarrhea by binding to and stimulating intestinal membrane-bound guanylyl cyclase, triggering production of cyclic GMP. Agents which stimulate protein kinase C (PKC), including phorbol esters, synergistically enhance STa effects on cGMP and