407721
m-Iodobenzylguanidine, Hemisulfate - CAS 80663-95-2 - Calbiochem
Synonym(s):
3-Iodobenzylguanidine, Hemisulfate, MIBG
assay
≥99% (HPLC)
form
solid
color
colorless to white
solubility
H2O: 20 mg/mL
General description
A cell-permeable norepinephrine analog that displays antiproliferative and proapoptotic properties. Reported to competitively inhibit arginine-dependent mono-ADP-ribosylation, impair mitochondrial respiration, stimulate glycolysis, and prevent terminal differentiation of skeletal myoblasts reversibly. Readily taken up by tissues rich in sympathetic neurons and neuroendocrine neoplasm via norepinephrine transporters (NET). Inhibits the phosphorylation of the Rho effector, PRK1/2 with no effect on the stimulation of MAP and PI-3 kinases.
Biochem/physiol Actions
Arginine-dependent mono-ADP-ribosylation
Preparation Note
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Storage Class
10-13 - German Storage Class 10 to 13
Regulatory Information
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L Smets et al.
Leukemia research, 12(9), 737-743 (1988-01-01)
Meta-iodo-benzylguanidine (MIBG; 3 x 10(-5) M), a novel inhibitor of mono(ADP-ribosylation)-and the general ribosylation inhibitor nicotinamide (NA; 5-20 mM) both stimulated the glucocorticoid-mediated lysis of sensitive L1210 leukemia cells and even induced susceptibility in various human and murine lines refractory
Michael Höpfner et al.
International journal of cancer, 101(3), 210-216 (2002-09-05)
Neuroendocrine gastrointestinal tumors take up, decarboxylate and store large amounts of monoamines. Radioactive-labeled monoamines like the norepinephrine analogue meta-iodobenzylguanidine (MIBG) have been used for the imaging of neuroendocrine tumors for many years. MIBG is selectively taken up via norepinephrine transporters
Lorraine Yau et al.
European journal of biochemistry, 270(1), 101-110 (2002-12-21)
ADP-ribosylation has been coupled to intracellular events associated with smooth muscle cell vasoreactivity, cytoskeletal integrity and free radical damage. Additionally, there is evidence that ADP-ribosylation is required for smooth muscle cell proliferation. Our investigation employed selective inhibitors to establish that
Lorraine Yau et al.
Experimental cell research, 301(2), 320-330 (2004-11-09)
The development of skeletal muscle is controlled by a highly synchronized series of cellular events, and various signals from both inside and outside the cell play a role in the switch from multipotential mesodermal stem cells to muscle fibers. Meta-iodobenzylguanidine
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