Hemin chloride
(Synonyms: 氯化血红素; Hemin chloride) 目录号 : GC14591
An oxidized form of heme
Cas No.:16009-13-5
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
| Cell experiment [1]: | |
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Cell lines |
LNCaP cells |
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Preparation Method |
Real-time PCR amplification of the total DNA from M. hyorhinis -infected LNCaP cells cultured for 48 h in the presence of varying concentrations of Hemin chloride. |
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Reaction Conditions |
100 µM Hemin chloride for 48 h |
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Applications |
Hemin chloride treatment induces HO-1 expression and inhibits M. hyorhinis replication in LNCaP prostate cancer cells. |
| Animal experiment [2]: | |
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Animal models |
C57BL/6 mice |
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Preparation Method |
House dust mite (HDM)-sensitized and challenged mice were instilled intranasally with 100 µg Hemin chloride-DCEVs at 1 d before sensitization and challenge. |
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Dosage form |
100 µg Hemin chloride-DCEVs at 1day |
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Applications |
In HDM-induced asthmatic mouse model, Hemin chloride-DCEVs inhalation reduced eosinophils infiltration and mucus secretion in the airway, decreased the levels of IL-4, IL-5, and IL-13 in the lung and the number of Th2 cells in mediastinal lymph nodes (MLNs), and increased the number of Treg cells in MLNs. |
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References: [1]. Huang H, Dabrazhynetskaya A, et,al. Hemin chloride activation abrogates Mycoplasma hyorhinis replication in chronically infected prostate cancer cells via heme oxygenase-1 induction. FEBS Open Bio. 2021 Oct;11(10):2727-2739. doi: 10.1002/2211-5463.13271. Epub 2021 Sep 9. PMID: 34375508; PMCID: PMC8487054. |
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Hemin chloride, a substrate of heme oxygenase (HO)-1, induces HO-1 expression on a variety of cells to exert anti-oxidant and anti-inflammatory roles.
A dramatic reduction of cell-associated M. hyorhinis DNA in a dose-dependent manner, with > 90% inhibition at 100 μm Hemin chloride. Hemin chloride treatment profoundly inhibited intracellular M. hyorhinis DNA levels within 10 h to nearly undetectable levels after 48 h[1]. Macrophage exposed to Hemin chloride exhibits modulation of non-opsonic phagocytosis of aged RBCs, ability to kill bacteria and secretion of cytokines.Translocation and sequestration of CD36 within the intracellular storage in the Hemin chloride treated macrophages. It in-turn modulates the global cytokine secretion from macrophages. CD36 has strong affinity for Hemin chloride with a dissociation constant of 1.26 ±0.24 μM[3]. Hemin chloride treatment decreased cell proliferation to 62.5 %, 51.3 %, and 38.8 % in PA-TU-8902, BxPC-3 and MiaPaCa-2 cancer cells, respectively. Enhancement of anti-proliferative effects of statins by Hemin chloride, documented as decreased cell proliferation after 48 h of co-treatment[5]. The presence of Hemin chloride in irradiated lung cancer cells enhanced the productivity of initial ROS, resulting in lipid peroxidation and subsequent ferroptosis[6].
In HDM-induced asthmatic mouse model, Hemin chloride-DCEVs inhalation reduced eosinophils infiltration and mucus secretion in the airway, decreased the levels of IL-4, IL-5, and IL-13 in the lung and the number of Th2 cells in mediastinal lymph nodes (MLNs), and increased the number of Treg cells in MLNs[2]. Hemin chloride-preconditioned mice exhibited preserved renal cell function, and the tubular injury score at 72h indicated that tubular damage was prevented[4]. When compared with wild-type littermates, the mortality for SS Cttn+/- mice trended to be lower after Hemin chloride infusion and these mice exhibited less severe lung injury and less necroptotic cell death[7].
References:
[1]. Huang H, Dabrazhynetskaya A, et,al.Hemin chloride activation abrogates Mycoplasma hyorhinis replication in chronically infected prostate cancer cells via heme oxygenase-1 induction. FEBS Open Bio. 2021 Oct;11(10):2727-2739. doi: 10.1002/2211-5463.13271. Epub 2021 Sep 9. PMID: 34375508; PMCID: PMC8487054.
[2]. Wu Y, Yu Q, et,al.Hemin chloride-primed dendritic cells suppress allergic airway inflammation through releasing extracellular vesicles. J Leukoc Biol. 2022 Apr;111(4):837-848. doi: 10.1002/JLB.3A0321-175R. Epub 2021 Jul 23. PMID: 34296788; PMCID: PMC9292814.
[3]. Banesh S, Layek S, et,al. Hemin chloride acts as CD36 ligand to activate down-stream signalling to disturb immune responses and cytokine secretion from macrophages. Immunol Lett. 2022 Mar;243:1-18. doi: 10.1016/j.imlet.2022.01.004. Epub 2022 Jan 31. PMID: 35104496.
[4]. Chen HH, Lu PJ, et,al. Heme oxygenase-1 ameliorates kidney ischemia-reperfusion injury in mice through extracellular signal-regulated kinase 1/2-enhanced tubular epithelium proliferation. Biochim Biophys Acta. 2015 Oct;1852(10 Pt A):2195-201. doi: 10.1016/j.bbadis.2015.07.018. Epub 2015 Jul 30. PMID: 26232688.
[5]. Vanova K, Boukalova S, et,al. Heme oxygenase is not involved in the anti-proliferative effects of statins on pancreatic cancer cells. BMC Cancer. 2016 May 12;16:309. doi: 10.1186/s12885-016-2343-9. PMID: 27175805; PMCID: PMC4866069.
[6]. Almahi WA, Yu KN, et,al. Hemin chloride enhances radiosensitivity of lung cancer cells through ferroptosis. Exp Cell Res. 2022 Jan 1;410(1):112946. doi: 10.1016/j.yexcr.2021.112946. Epub 2021 Nov 24. PMID: 34826424.
[7]. Jones NM, Sysol JR,et,al. Cortactin loss protects against Hemin chloride-induced acute lung injury in sickle cell disease. Am J Physiol Lung Cell Mol Physiol. 2022 Jun 1;322(6):L890-L897. doi: 10.1152/ajplung.00274.2021. Epub 2022 May 3. PMID: 35503995; PMCID: PMC9169831.
氯化血红素是血红素加氧酶(HO)-1的底物，可诱导多种细胞表达HO-1，发挥抗氧化和抗炎作用。
细胞相关的猪鼻支原体 DNA 以剂量依赖性方式显着减少，>；在 100 μm 氯化血红素下有 90% 的抑制。氯化血红素处理可在 10 小时内显着抑制细胞内猪鼻支原体 DNA 水平，48 小时后几乎检测不到[1]。暴露于氯化血红素的巨噬细胞表现出对老化红细胞的非调理吞噬作用的调节、杀灭细菌的能力和细胞因子的分泌。CD36 在氯化血红素处理的巨噬细胞的细胞内储存中的易位和隔离。它反过来调节巨噬细胞的整体细胞因子分泌。 CD36 对氯化血红素具有很强的亲和力，解离常数为 1.26 ±0.24 μM[3]。氯化血红素处理将 PA-TU-8902、BxPC-3 和 MiaPaCa-2 癌细胞的细胞增殖分别降低至 62.5%、51.3% 和 38.8%。氯化血红素增强他汀类药物的抗增殖作用，记录为联合治疗 48 小时后细胞增殖减少[5]。受照射的肺癌细胞中氯化血红素的存在增强了初始 ROS 的生产力，导致脂质过氧化和随后的铁死亡[6]。
在 HDM 诱导的哮喘小鼠模型中，氯化血红素-DCEVs 吸入减少了气道中的嗜酸性粒细胞浸润和粘液分泌，降低了肺中 IL-4、IL-5 和 IL-13 的水平以及 Th2 的数量纵隔淋巴结 (MLN) 中的细胞，并增加 MLN 中 Treg 细胞的数量[2]。氯化血红素预处理小鼠的肾细胞功能得到保护，72 小时的肾小管损伤评分表明肾小管损伤得到了预防[4]。与野生型同窝小鼠相比，SS Cttn+/- 小鼠在输注氯化血红素后死亡率趋于降低，并且这些小鼠表现出较轻的肺损伤和较少的坏死性细胞死亡[7]。
| Cas No. | 16009-13-5 | SDF | |
| 别名 | 氯化血红素; Hemin chloride | ||
| 化学名 | (SP-5-13)-chloro[7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,8-dipropanoato(4-)-κN21, κN22, κN23, κN24]-ferrate(2-), dihydrogen | ||
| Canonical SMILES | [O-]C(CCC1=C(C=C2[N]3=C4C(C)=C2CCC([O-])=O)[N-]([Fe+3]35([Cl-])[N]6=C7C=C(C(C=C)=C8C)[N-]5C8=C4)C(C=C6C(C=C)=C7C)=C1C)=O.[H+].[H+] | ||
| 分子式 | C34H30ClFeN4O4 • 2H | 分子量 | 652.0 |
| 溶解度 | 17.33 mg/mL in DMSO,2.5 mg/mL in NH4OH,0.1 mg/mL in Water | 储存条件 | 4°C, protect from light, stored under nitrogen |
| 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 | 1.5337 mL | 7.6687 mL | 15.3374 mL |
| 5 mM | 0.3067 mL | 1.5337 mL | 3.0675 mL |
| 10 mM | 0.1534 mL | 0.7669 mL | 1.5337 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。
Exogenous Hemin alleviated cadmium stress in maize ( Zea mays L.) by enhancing leaf photosynthesis, AsA-GSH cycle and polyamine metabolism
Cadmium (Cd) stress is one of the principal abiotic stresses that inhibit maize growth. The research was to explore (hemin chloride) Hemin (100 μmol L-1) on photosynthesis, ascorbic acid (AsA)-glutathione (GSH) cycle system, and polyamine metabolism of maize under Cd stress (85 mg L-1) using nutrient solution hydroponics, with Tiannong 9 (Cd tolerant) and Fenghe 6 (Cd sensitive) as experimental materials. The results showed that Hemin can increase leaf photosynthetic pigment content and ameliorate the ratio of Chlorophyll a/chlorophyll b (Chla/Chlb) under Cd stress. The values of ribose 1, 5-diphosphate carboxylase/oxygenase (RuBPcase) and phosphoenolpyruvate carboxylase (PEPCase), and total xanthophyll cycle pool [(violoxanthin (V), antiflavin (A) and zeaxanthin (Z)] increased, which enhancing xanthophyll cycle (DEPS) de-epoxidation, and alleviating stomatal and non-stomatal limitation of leaf photosynthesis. Hemin significantly increased net photosynthetic rate (Pn ), stomatal conductance (gs ), transpiration rate (Tr ), photochemical quenching coefficient (qP), PSII maximum photochemical efficiency (Fv/Fm ), and electron transfer rate (ETR), which contributed to the improvement of the PSII photosynthetic system. Compared with Cd stress, Hemin can reduce thiobartolic acid reactant (TBARS) content, superoxide anion radical (O2 -) production rate, hydrogen peroxide (H2O2) accumulation, and the extent of electrolyte leakage (EL); decreased the level of malondialdehyde (MDA) content and increased the activities of superoxide dismutase (SOD), peroxidase (POD) and catalase (CAT); slowed the decrease in dehydroascorbic acid reductase (DHAR) and monodehydroascorbate reductase (MDHAR) activity and the increase in glutathione reductase (GR) and ascorbate peroxidase (APX) activity in leaves; promoted the increase in AsA and GSH content, decreased dehydroascorbic acid (DHA) and oxidized glutathione (GSSG), and increased AsA/DHA and GSH/GSSG ratios under Cd stress. Hemin promoted the increase of conjugated and bound polyamine content, and the conversion process speed of free putrescine (Put) to free spermine (Spm) and spermidine (Spd) in maize; decreased polyamine oxidase (PAO) activity and increased diamine oxidase (DAO), arginine decarboxylase (ADC), ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (SAMDC) enzyme activities in leaves under Cd stress.
Effect of myoglobin, hemin, and ferric iron on quality of chicken breast meat
Objective: The objective was to evaluate the impact of different forms of iron including myoglobin, hemin, and ferric chloride on the quality of chicken breast meat.
Methods: Chicken breast muscles were subjected to 1, 2, 3 mg/mL of FeCl3, myoglobin and hemin treatment respectively, and the production of reactive oxygen species (ROS) and malondialdehyde, meat color, tenderness, water holding capacity and morphology of meat was evaluated.
Results: Hemin was found to produce more ROS and induce greater extent of lipid oxidation than myoglobin and ferric chloride. However, it showed that hemin could significantly increase the redness and decrease the lightness of the muscle. Hemin was also shown to be prominent in improving water holding capacity of meat, maintaining a relatively higher level of the immobilized water from low-field nuclear magnetic resonance measurements. Morphology observation by hematoxylin-eosin staining further confirmed the results that hemin preserved the integrity of the muscle.
Conclusion: The results indicated that hemin may have economic benefit for the industry based on its advantage in improving water holding capacity and quality of meat.
Hemin induces active chloride secretion in Caco-2 cells
Enterocytes maintain fluid-electrolyte homeostasis by keeping a tight barrier and regulating ion channels. Carbon monoxide (CO), a product of heme degradation, modulates electrolyte transport in kidney and lung epithelium, but its role in regulating intestinal fluid-electrolyte homeostasis has not been studied. The major source of endogenous CO formation comes from the degradation of heme via heme oxygenase. We hypothesized that heme activates electrolyte transport in intestinal epithelial cells. Basolateral hemin treatment increased baseline Caco-2 cell short-circuit currents (I(sc)) twofold (control = 1.96 +/- 0.14 microA/cm(2) vs. hemin = 4.07 +/- 0.16 microA/cm(2), P < 0.01); apical hemin had no effect. Hemin-induced I(sc) was caused by Cl- secretion because it was inhibited in Cl- -free medium, with ouabain, 5-nitro-2-(3-phenylpropylamino) benzoic acid (NPPB), or DIDS. Apical electrogenic Na+ channel inhibitor benzamil had no effect on hemin-induced I(sc). Hemin did not alter the ability of Caco-2 cells to respond maximally to forskolin, but a soluble guanylate cyclase inhibitor, [1,2,4]oxadiazolo-[4,3-a]quinoxalin-1-one (ODQ) inhibited the effects of hemin. A CO-releasing molecule, tricarbonyldichlororuthenium II, induced active Cl- secretion that was also inhibited with ODQ. We conclude that hemin induces active Cl- secretion in Caco-2 cells via a cGMP-dependent pathway. These effects are probably the consequence of CO formation. Heme and CO may be important regulators of intestinal fluid-electrolyte homeostasis.
Hemin lyses malaria parasites
Malaria parasites isolated from mouse erythrocytes are lysed by ferriprotoporphyrin IX chloride (hemin) or by a chloroquine-hemin complex in amounts that could be produced by release of less than 0.1 percent of the heme in erythrocytic hemoglobin. This effect of hemin may explain the protection against malaria provided by thalassemia and other conditions causing intracellular denaturation of hemoglobin. The toxicity of the chloroquine-hemin complex may explain the selective antimalarial action of chloroquine.
Hemin-mediated DNA strand scission
Hemin (ferric protoporphyrin IX chloride) has been shown to cause strand scission in DNA in a reaction which requires the presence of oxygen and the reducing agent, 2-mercaptoethanol. In model studies, circular supercoiled plasmid DNA is converted within 30 min to the open circle and linear forms. With longer incubation times the DNA is degraded to small pieces. The reaction is markedly influenced by the addition of divalent cations; Mg2+ and Ca2+ inhibit the reaction while the transition metals Co2+, Zn2+, Ni2+, and Cu2+ promote the degradation. These observations are discussed in relation to the role of hemin in the modulation of gene expression during cell differentiation.