Cobaltic Protoporphyrin IX (chloride)
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Overview
Regulatory Status: RUO
Shipping:
cool pack
Storage:
-20℃
Documents
Further Information
Bioactivity:
Cobaltic protoporphyrin IX is a metalloporphyrin and an inducer of heme oxygenase-1 (HO-1) activity.1Unlike other metalloporphyrins, cobaltic protoporphyrin IX induces activity of HO-1, the rate-limiting enzyme in heme catabolism,in vitroandin vivo.1,2It also reduces the activity of δ-aminolevulinate synthase, the enzyme that catalyzes the rate-limiting step of heme biosynthesis, as well as decreases the activity of cytochrome P450 (CYP), in rat liver microsomesex vivowhen administered at a dose of 125 μmol/kg.2Cobaltic protoporphyrin IX (5 mg/kg) prevents liver injury and increases in the percentage of hepatic apoptotic cells in a mouse model of liver ischemia-reperfusion injury.3It increases survival and decreases the number of lung colony forming units (CFUs) in mice infected withY. pestisat the same dose.4Cobaltic protoporphyrin IX has also been used as a catalyst for the electrochemical reduction of carbon dioxide in carbon electrodes.5
CAS:
102601-60-5
Formula:
C34H30ClCoN4O4?2H
Molecular Weight:
655
Purity:
0.98
SMILES:
[Cl-][Co+3]1([N](C2=C3)=C(C(C=C)=C2C)C=C4C(C)=C5CCC([O-])=O)([N-]6C3=C7C=C)[N-]4C5=CC(C(CCC([O-])=O)=C8C)=[N]1C8=CC6=C7C.[H+].[H+]
References
Willix, J.L., Stockton, J.L., Olson, R.M., et al.Activation of heme oxygenase expression by cobalt protoporphyrin treatment prevents pneumonic plague caused by inhalation of Yersinia pestisAntimicrob. Agents Chemother.64(4)e01819-01819(2020)
Shen, J., Kortlever, R., Kas, R., et al.Electrocatalytic reduction of carbon dioxide to carbon monoxide and methane at an immobilized cobalt protoporphyrinNat. Commun.68177(2015)
Shan, Y., Lambrecht, R.W., Donohue, S.E., et al.Role of Bach1 and Nrf2 in up-regulation of the heme oxygenase-1 gene by cobalt protoporphyrinFASEB J.20(14)2651-2653(2006)
Li, J., Wu, B., Teng, D., et al.Cobalt-protoporphyrin enhances heme oxygenase 1 expression and attenuates liver ischemia/reperfusion injury by inhibiting apoptosisMol. Med. Rep.17(3)4567-4572(2018)
Drummond, G.S., and Kappas, A.The cytochrome P-450-depleted animal: An experimental model for in vivo studies in chemical biologyProc. Natl. Acad. Sci. USA79(7)2384-2388(1982)