Peroxidase
(Synonyms: 过氧化物酶（辣根）) 目录号 : GC61846
Peroxidase在氧化活性氧、先天免疫、激素生物合成和多种疾病的发病机制等方面具有重要作用。
Cas No.:9003-99-0
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
Peroxidase actively involves in oxidizing reactive oxygen species, innate immunity, hormone biosynthesis and pathogenesis of several diseases[1].
Peroxidases belong to a large family of isoenzymes present in almost all living organisms. These are generally heme containing enzymes ranging in Mw from 35-100 Kd. Mammalian peroxidases are much larger proteins (576-738 amino acids) than the plant counterparts. Peroxidases exist as monomers, dimmers or tetramers and their gene locations also vary among different chromosomes. Peroxidases have some organ, tissue, cellular and sub-cellular specific distribution patterns, performing some specific functions[1].
References:
[1]. Khan AA, et al. Biochemical and pathological studies on peroxidases -an updated review. Glob J Health Sci. 2014 May 13;6(5):87-98.
| Cas No. | 9003-99-0 | SDF | |
| 别名 | 过氧化物酶（辣根） | ||
| Canonical SMILES | [Peroxidase] | ||
| 分子式 | 分子量 | ||
| 溶解度 | 0.1 M phosphate buffer: soluble 10 mg/mL, clear, orange to red (pH 6.0) | 储存条件 | Store at -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。 | ||
| 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。
2D material-based peroxidase-mimicking nanozymes: catalytic mechanisms and bioapplications
Anal Bioanal Chem 2022 Apr;414(9):2971-2989.PMID:35234980DOI:10.1007/s00216-022-03985-w.
The boom in nanotechnology brings new insights into the development of artificial enzymes (nanozymes) with ease of modification, lower manufacturing cost, and higher catalytic stability than natural enzymes. Among various nanomaterials, two-dimensional (2D) nanomaterials exhibit promising enzyme-like properties for a plethora of bioapplications owing to their unique physicochemical characteristics of tuneable composition, ultrathin thickness, and huge specific surface area. Herein, we review the recent advances in several 2D material-based nanozymes, such as carbonaceous nanosheets, metal-organic frameworks (MOFs), transition metal dichalcogenides (TMDs), layered double hydroxides (LDHs), and transition metal oxides (TMOs), clarify the mechanisms of Peroxidase (POD)-mimicking catalytic behaviors, and overview the potential bioapplications of 2D nanozymes.
Peroxidase Activity of Human Hemoproteins: Keeping the Fire under Control
Molecules 2018 Oct 8;23(10):2561.PMID:30297621DOI:10.3390/molecules23102561.
The heme in the active center of peroxidases reacts with hydrogen peroxide to form highly reactive intermediates, which then oxidize simple substances called Peroxidase substrates. Human peroxidases can be divided into two groups: (1) True peroxidases are enzymes whose main function is to generate free radicals in the Peroxidase cycle and (pseudo)hypohalous acids in the halogenation cycle. The major true peroxidases are myeloperoxidase, eosinophil Peroxidase and lactoperoxidase. (2) Pseudo-peroxidases perform various important functions in the body, but under the influence of external conditions they can display peroxidase-like activity. As oxidative intermediates, these peroxidases produce not only active heme compounds, but also protein-based tyrosyl radicals. Hemoglobin, myoglobin, cytochrome c/cardiolipin complexes and cytoglobin are considered as pseudo-peroxidases. Рeroxidases play an important role in innate immunity and in a number of physiologically important processes like apoptosis and cell signaling. Unfavorable excessive Peroxidase activity is implicated in oxidative damage of cells and tissues, thereby initiating the variety of human diseases. Hence, regulation of Peroxidase activity is of considerable importance. Since peroxidases differ in structure, properties and location, the mechanisms controlling Peroxidase activity and the biological effects of Peroxidase products are specific for each hemoprotein. This review summarizes the knowledge about the properties, activities, regulations and biological effects of true and pseudo-peroxidases in order to better understand the mechanisms underlying beneficial and adverse effects of this class of enzymes.
Recent advances in biomedical applications of 2D nanomaterials with peroxidase-like properties
Adv Drug Deliv Rev 2022 Jun;185:114269.PMID:35398244DOI:10.1016/j.addr.2022.114269.
Significant progress has been made in developing two-dimensional (2D) nanomaterials owing to their ultra-thin structure, high specific surface area, and many other advantages. Recently, 2D nanomaterials with enzyme-like properties, especially Peroxidase (POD)-like activity, are highly desirable for many biomedical applications. In this review, we first classify the types of 2D POD-like nanomaterials and then summarize various strategies for endowing 2D nanomaterials with POD-like properties. Representative examples of biomedical applications are reviewed, emphasizing in antibacterial, biosensing, and cancer therapy. Last, the future challenges and prospects of 2D POD-like nanomaterials are discussed. This review is expected to provide an in-depth understanding of 2D POD-like materials for biomedical applications.
Surface acidity modulates the peroxidase-like activity of nanoclay
Chem Commun (Camb) 2022 Oct 4;58(79):11135-11138.PMID:36106489DOI:10.1039/d2cc04213d.
A novel surface acidity modulation strategy allows us to obtain modified nanoclay with specific Peroxidase (POD)-like catalytic activity. Fe3+ exchange could increase the surface acidity of modified montmorillonite (MMT), resulting in a significant enhancement of its POD-like activity. We proposed that the POD-like catalytic reaction followed the electron transfer pathway and ping-pong mechanism. Correspondingly the constructed colorimetric sensor for H2O2 exhibited high sensitivity and specificity.
Modular Peroxidase-Based Reporters for Detecting Protease Activity and Protein Interactions with Temporal Gating
J Am Chem Soc 2022 Dec 21;144(50):22933-22940.PMID:36511757DOI:10.1021/jacs.2c08280.
Enzymatic reporters have been widely applied to study various biological processes because they can amplify signal through enzymatic reactions and provide good sensitivity. However, there is still a need for modular motifs for designing a series of enzymatic reporters. Here, we report a modular peroxidase-based motif, named CLAPon, that features acid-base coil-caged enhanced ascorbate Peroxidase (APEX). We demonstrate the modularity of CLAPon by designing a series of reporters for detecting protease activity and protein-protein interactions (PPIs). CLAPon for protease activity showed a 390-fold fluorescent signal increase upon tobacco etch virus protease cleavage. CLAPon for PPI detection (PPI-CLAPon) has two variants, PPI-CLAPon1.0 and 1.1. PPI-CLAPon1.0 showed a signal-to-noise ratio (SNR) of up to 107 for high-affinity PPI pairs and enabled imaging with sub-cellular spatial resolution. However, the more sensitive PPI-CLAPon1.1 is required for detecting low-affinity PPI pairs. PPI-CLAPon1.0 was further engineered to a reporter with light-dependent temporal gating, called LiPPI-CLAPon1.0, which can detect a 3-min calcium-dependent PPI with an SNR of 17. LiPPI-CLAPon enables PPI detection within a specific time window with rapid APEX activation and diverse readout. Lastly, PPI-CLAPon1.0 was designed to have chemical gating, providing more versatility to complement the LiPPI-CLAPon. These CLAPon-based reporter designs can be broadly applied to study various signaling processes that involve protease activity and PPIs and provide a versatile platform to design various genetically encoded reporters.