Cobaltic Protoporphyrin IX (chloride)
(Synonyms: 原卟啉氯化钴) 目录号 : GC49096
An inducer of HO-1 activity
Cas No.:102601-60-5
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >95.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Cobaltic protoporphyrin IX is a metalloporphyrin and an inducer of heme oxygenase-1 (HO-1) activity.1 Unlike other metalloporphyrins, cobaltic protoporphyrin IX induces activity of HO-1, the rate-limiting enzyme in heme catabolism, in vitro and in vivo.1,2 It 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 microsomes ex vivo when administered at a dose of 125 µmol/kg.2 Cobaltic 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.3 It increases survival and decreases the number of lung colony forming units (CFUs) in mice infected with Y. pestis at the same dose.4 Cobaltic protoporphyrin IX has also been used as a catalyst for the electrochemical reduction of carbon dioxide in carbon electrodes.5
1.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) 2.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) 3.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) 4.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) 5.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)
| Cas No. | 102601-60-5 | SDF | |
| 别名 | 原卟啉氯化钴 | ||
| Canonical 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+] | ||
| 分子式 | C34H30ClCoN4O4·2H | 分子量 | 655 |
| 溶解度 | DMF: 30 mg/ml,DMF:PBS (pH 7.2) (1:6): 0.14 mg/ml,DMSO: 25 mg/ml,Ethanol: 1 mg/ml | 储存条件 | -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 1.5267 mL | 7.6336 mL | 15.2672 mL |
| 5 mM | 0.3053 mL | 1.5267 mL | 3.0534 mL |
| 10 mM | 0.1527 mL | 0.7634 mL | 1.5267 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
The effect of the administration of Cobaltic Protoporphyrin IX on drug metabolism, carbon tetrachloride activation and lipid peroxidation in rat liver microsomes
Chem Biol Interact 1984 Jul;50(2):143-51.PMID:6430572DOI:10.1016/0009-2797(84)90091-7.
The effects of Cobaltic Protoporphyrin IX (CPP) administration on hepatic microsomal drug metabolism, carbon tetrachloride activation and lipid peroxidation have been investigated using male Wistar rats. CPP (125 mumol/kg, 72 h before sacrifice) profoundly decreased the levels of hepatic microsomal heme, particularly cytochrome P-450. Consequently, the associated mixed-function oxidase systems were equally strongly depressed. An unexpected finding was that CPP administration also greatly decreased the activity of NADPH/cytochrome c reductase, a result not generally found with the administration of the more widely used cytochrome P-450 depleting agents, cobaltous chloride. Activation of carbon tetrachloride, measured as covalent binding of [14C] CCl4, spin-trapping of CCl3 and CCl4-stimulated lipid peroxidation, was much lower in liver microsomes from CPP-treated rats. Other microsomal lipid peroxidation systems, utilising cumene hydroperoxide or NADPH/ADP-Fe2+, were also depressed in parallel with the decrease in microsomal enzyme activities.
Co(III) protoporphyrin IX chloride in solution: spin-state and metal coordination revealed from resonant inelastic X-ray scattering and electronic structure calculations
Phys Chem Chem Phys 2015 Feb 7;17(5):3409-14.PMID:25529387DOI:10.1039/c4cp04703f.
The local electronic structure of the cobalt centre-ion of Co(III) protoporphyrin IX chloride dissolved in dimethyl sulfoxide (DMSO) liquid solution is studied by resonant inelastic X-ray scattering (RIXS) spectroscopy at the cobalt L-edge. The resulting cobalt 2p partial-fluorescence-yield (PFY) X-ray absorption (XA) spectrum, integrated from RIXS spectra, is simulated for various possible spin-states and coordination of the cobalt centre by using the newly developed density functional theory/restricted open shell single excitation configuration interaction (DFT/ROCIS) method. Comparison between experiment and calculation shows that the cobalt ion (3d(6) electronic configuration) adopts a low-spin state with all six 3d electrons paired, and the cobalt centre is either 5-coordinated by its natural ligands (one chloride ion and four nitrogen atoms), or 6-coordinated, when binding to an oxygen atom of a DMSO solvent molecule. Analysis of the measured RIXS spectra reveals weak 3d-3d electron correlation, and in addition a value of the local HOMO-LUMO gap at the Co sites is obtained.
Gold Nanoparticles/Nanographene-Based 3D Sensors Integrated in Mini-Platforms for Thiamine Detection
Sensors (Basel) 2022 Dec 29;23(1):344.PMID:36616942DOI:10.3390/s23010344.
Vitamins are essential for sustaining daily activities and perform crucial roles in metabolism, such as preventing vascular events and delaying the development of diabetic nephropathy. The ultrasensitive assessment of thiamine in foods is required for food quality evaluation. A mini-platform utilizing two 3D sensors based on nanographene and gold nanoparticles paste modified with protoporphyrin IX and protoporphyrin IX cobalt chloride is proposed for the detection of thiamine in blueberry syrup, multivitamin tablets, water, and a biological sample (urine). Differential pulse voltammetry was utilized for the characterization and validation of the suggested sensors. The sensor modified with protoporphyrin IX has a detection limit of 3.0 × 10-13 mol L-1 and a quantification limit of 1.0 × 10-12 mol L-1, whereas the sensor modified with protoporphyrin IX cobalt chloride has detection and quantification limits of 3.0 × 10-12 and 1.0 × 10-11 mol L-1, respectively. High recoveries (values greater than 95.00%) and low RSD (%) values (less than 5.00%) are recorded for both 3D sensors when used for the determination of thiamine in blueberry syrup, multivitamin tablets, water, and urine, demonstrating the 3D sensors' and suggested method's high reliability.
Heme oxygenase induction by CoCl2, Co-protoporphyrin IX, phenylhydrazine, and diamide: evidence for oxidative stress involvement
Arch Biochem Biophys 1991 May 1;286(2):610-7.PMID:1716866DOI:10.1016/0003-9861(91)90088-z.
The induction of heme oxygenase in rat liver by cobaltous chloride (CoCl2) and Co-protoporphyrin IX is entirely prevented by the administration of alpha-tocopherol and allopurinol. CoCl2 was converted in the liver into Co-protoporphyrin IX before it induced heme oxygenase activity. Actinomycin and cycloheximide affected to a similar degree the induction of heme oxygenase by both CoCl2 and Co-protoporphyrin IX. Administration of either CoCl2 or Co-protoporphyrin strongly decreased the intrahepatic GSH pool, a decrease which was completely prevented by the administration of either alpha-tocopherol or allopurinol. The latter compounds prevented heme oxygenase induction as well as the decrease in hepatic GSH when administered 2 h before, together with, or 2 h after CoCl2. However, when given 5 h after administration of CoCl2, alpha-tocopherol and allopurinol showed no preventive effect. Similar results were obtained when Co-protoporphyrin IX was used, with the difference that when alpha-tocopherol and allopurinol were given 2 h after administration of the inducer, they showed no protective effect. Phenylhydrazine and diamide also induced heme oxygenase activity in rat liver. This inductive effect was preceded by a decrease in the intrahepatic GSH pool, which took place several hours before induction of the oxygenase. Administration of alpha-tocopherol and allopurinol prevented induction of the oxygenase but had no effect on the decrease in GSH levels. These results suggest that the induction of heme oxygenase by phenylhydrazine and the diamide is preceded by an oxidative stress which very likely originates in the depletion of GSH. The induction of heme oxygenase by hemin was not prevented by administration of alpha-tocopherol or allopurinol. Coprotoporphyrin IX did not affect the pattern of the molecular forms of hepatic biliverdin reductase, at variance with CoCl2, which is known to convert molecular form 1 of the enzyme into molecular form 3.
Evidence for the involvement of heme oxygenase-1 in the antidepressant-like effect of zinc
Pharmacol Rep 2017 Jun;69(3):497-503.PMID:28342333DOI:10.1016/j.pharep.2017.01.010.
Background: Considering that heme oxygenase-1 (HO-1) and the brain-derived neurotrophic factor (BDNF)-mediated pathway are involved in the pathophysiology of depression and that zinc has been shown to exert beneficial effects in the management of depression, this study investigated the influence of these targets on the antidepressant-like effect of zinc. Methods: Mice were treated with sub-effective or effective doses of zinc chloride (ZnCl2, 10mg/kg, po), and 45min later, they received intracerebroventricular (icv) injections of sub-effective doses of either zinc protoporphyrin IX (ZnPP, 10μg/mouse, HO-1 inhibitor), cobalt protoporphyrin IX (CoPP, 0.01μg/mouse, HO-1 inducer) or K-252a (1μg/mouse, TrkB receptor antagonist). Immobility time and locomotor activity were evaluated through the tail suspension test (TST) and open-field test (OFT), respectively. HO-1 immunocontents were evaluated in the prefrontal cortex and hippocampus 60min after ZnCl2 (10mg/kg, po) treatment. Results: The antidepressant-like effect of ZnCl2 was prevented by the treatment with ZnPP and K-252a. Furthermore, sub-effective doses of CoPP and ZnCl2 produced a synergistic antidepressant-like effect in the TST. None of the treatments altered locomotor activity. ZnCl2 administration increased HO-1 immunocontents only in the prefrontal cortex. Conclusions: The results indicate that the antidepressant-like effect of ZnCl2 in the TST may depend on the induction of HO-1, and activation of TrkB receptor.