POB | Ornithine decarboxylase inhibitor
NMR (Confirms)
Available Options
| Size : | Price | Quantity | |
|---|---|---|---|
| 10 mg | $70.00 | ||
| 50 mg | $260.00 |
POB (946135-39-3) is a transition state-based, cell permeable pro-drug inhibitor of ODC, a key enzyme involved in polyamine synthesis and a potential cancer drug target. Intracellularly, POB is phosphorylated by pyridoxal kinase and the methyl ester hydrolyzed. This active inhibitor most likely binds apo-ODC resulting in greatly reduced ODC activity and inhibition of cellular proliferation. POB was able to inhibit proliferation in a wide variety of tumor cell lines: LN229 (IC50 = 50 μM), Jurkat, COS7, SW2 and both high and low-grade glioblastoma multiforme. More potent than DFMO.
References/Citations:
1) Wu et al. (2007), New transition state-based inhibitor for human ornithine decarboxylase inhibits growth of tumor cells; Mol. Cancer Ther., 6 1831
2) Wu et al. (2011), A novel approach to inhibit intracellular vitamin B6-dependent enzymes: proof of principle with human and plasmodium ornithine decarboxylase and human histidine decarboxylase; FASEB J., 25 2109
NMR (Confirms)
Safety Data Sheet:
Product Data Sheet:
Materials provided by Focus Biomolecules are for laboratory research use only and are not intended for human or veterinary applications. Please note that we do not sell to individuals and that all orders placed by non-research organizations will incur a $20 restocking/refund fee
POB (946135-39-3) is a transition state-based, cell permeable pro-drug inhibitor of ODC, a key enzyme involved in polyamine synthesis and a potential cancer drug target. Intracellularly, POB is phosphorylated by pyridoxal kinase and the methyl ester hydrolyzed. This active inhibitor most likely binds apo-ODC resulting in greatly reduced ODC activity and inhibition of cellular proliferation. POB was able to inhibit proliferation in a wide variety of tumor cell lines: LN229 (IC50 = 50 μM), Jurkat, COS7, SW2 and both high and low-grade glioblastoma multiforme. More potent than DFMO.
References/Citations:
1) Wu et al. (2007), New transition state-based inhibitor for human ornithine decarboxylase inhibits growth of tumor cells; Mol. Cancer Ther., 6 1831
2) Wu et al. (2011), A novel approach to inhibit intracellular vitamin B6-dependent enzymes: proof of principle with human and plasmodium ornithine decarboxylase and human histidine decarboxylase; FASEB J., 25 2109
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