Ceratotoxin A
目录号 : GC32323
CeratotoxinA是由29个氨基酸组成的多肽，从副腺分泌液中分离到，具有抗细菌(anti-bacterial)的作用。
Cas No.:150671-04-8
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
Ceratotoxin A, a 29-residue peptide isolated from the accessory gland secretion fluid, with strong anti-bacterial activity.
Ceratotoxin A is a 29-residue peptide isolated from the accessory gland secretion fluid, shows anti-E.coli activity, and is heat stable[1]. Ceratotoxin A is effective against Escherichia coli ATCC 23739, Pseudomonas aeruginos ATCC 27853, and Bacillus subtilis ATCC 6633 with minimal inhibitory concentration (MIC) of 7, 7, and 3.5 µM[2].
[1]. Marchini D, et al. Purification and primary structure of ceratotoxin A and B, two antibacterial peptides from the female reproductive accessory glands of the medfly Ceratitis capitata (Insecta:Diptera). Insect Biochem Mol Biol. 1993 Jul;23(5):591-8. [2]. Marri L, et al. The novel antibacterial peptide ceratotoxin A alters permeability of the inner and outer membrane of Escherichia coli K-12. Curr Microbiol. 1996 Jul;33(1):40-3.
| Cas No. | 150671-04-8 | SDF | |
| Canonical SMILES | Ser-Ile-Gly-Ser-Ala-Leu-Lys-Lys-Ala-Leu-Pro-Val-Ala-Lys-Lys-Ile-Gly-Lys-Ile-Ala-Leu-Pro-Ile-Ala-Lys-Ala-Ala-Leu-Pro | ||
| 分子式 | C135H243N35O32 | 分子量 | 2868.59 |
| 溶解度 | Soluble in DMSO | 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。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 0.3486 mL | 1.743 mL | 3.486 mL |
| 5 mM | 0.0697 mL | 0.3486 mL | 0.6972 mL |
| 10 mM | 0.0349 mL | 0.1743 mL | 0.3486 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。
Targeting specific membranes with an azide derivative of the pore-forming peptide Ceratotoxin A
Biochim Biophys Acta Biomembr 2019 Oct 1;1861(10):183023.PMID:31325418DOI:10.1016/j.bbamem.2019.07.011.
Pore-forming antimicrobial peptides (AMPs) are attracting interest as cytolytic antibiotics and drug delivery agents with potential use for targeting cancer cells or multidrug-resistant pathogens. Ceratotoxin A (CtxA) is an insect-derived cytolytic AMP with 36 amino acids that is thought to protect the eggs of the medfly Ceratitis capitata against pathogens. Single channel recordings using planar lipid bilayers have shown that CtxA forms pores with well-defined conductance states resembling those of alamethicin; it also forms one of the largest pores among the group of ceratotoxins. In this work, we modified CtxA at its N-terminus with an azide group and investigated its pore-forming characteristics in planar lipid bilayer experiments. We demonstrate the possibility to target specific lipids by carrying out click reactions in-situ on lipid membranes that display a dibenzocyclooctyne (DBCO) moiety on their head group. As a result of covalent linkage of the peptides to the bilayer, pore-formation occurs at 10-fold reduced peptide concentration and with a reduced dependence on the transmembrane voltage compared to unlinked CtxA-azide peptides or native CtxA peptides.
Molecular characterization of ceratotoxin C, a novel antibacterial female-specific peptide of the ceratotoxin family from the medfly Ceratitis capitata
Eur J Biochem 1996 Oct 15;241(2):330-7.PMID:8917427DOI:10.1111/j.1432-1033.1996.00330.x.
Ceratotoxins A and B are antibacterial peptides produced by the sexually mature females of Ceratitis capitata. The gene expression is restricted to the female reproductive accessory glands, and is not affected by bacterial infection, but is enhanced by mating. We report here the purification and the amino acid sequence of ceratotoxin C, a novel member of the ceratotoxin family, the cloning of its cDNA and the analysis of its expression. Ceratotoxin C is coordinately expressed with the other members of the ceratotoxin family. Its antibacterial activity is directed against both Gram-negative and Gram-positive bacterial strains but it is lower than that of Ceratotoxin A. We demonstrate in the genome of C. capitata the presence of at least three ceratotoxin genes which express, in the female accessory glands, a set of peptides presumably involved in the protection of the genital tract during fertilization.
The antibacterial peptide Ceratotoxin A displays alamethicin-like behavior in lipid bilayers
Peptides 2003 Nov;24(11):1779-84.PMID:15019210DOI:10.1016/j.peptides.2003.09.015.
Ceratotoxin A (CtxA), a 36-residue alpha-helical cationic peptide isolated from the medfly Ceratitis capitata, exhibits strong antibacterial activity. To determine its mode of action against bacteria, we investigated the behavior of Ceratotoxin A by incorporating it into planar lipid bilayers. Macroscopic and single channel conductance experiments showed that Ceratotoxin A forms voltage-dependent ion channels in bilayers according to the barrel-stave model. The characteristics of the channel suggest that the C-terminal regions form bundles of five or six helices embedded in the membrane, such that the N-terminal moieties lie on the polar side of the lipid bilayer.
Susceptibility of Rickettsia monacensis and Rickettsia peacockii to Cecropin A, Ceratotoxin A, and lysozyme
Curr Microbiol 2005 Oct;51(4):233-8.PMID:16132458DOI:10.1007/s00284-005-4532-7.
Ticks host obligate intracellular bacteria that range from benign symbiotes to virulent human pathogens. The effects on those bacteria of antimicrobial peptides (AMPs) involved in arthropod innate immunity to microbial infections are largely unknown. We evaluated effects of AMPs and a c-type lysozyme on host cell-free suspensions of the tick symbiotes Rickettsia monacensis and Rickettsia peacockii with stain-based infectivity and viability assays. Cecropin A at a concentration of 8 muM: had a lethal effect on both rickettsiae while Ceratotoxin A was approximately 20-fold less effective. Toxicity of both AMPs was synergized by lysozyme, an enzyme expressed by ticks. Lactoferrin, a transferrin, had no effect on R. monacensis at up to 110 microM. The rickettsiae were less sensitive to the AMPs than is typical of bacteria that grow extracellularly. Our assays may be useful in the study of AMP activity against other obligate intracellular bacteria.
The novel antibacterial peptide Ceratotoxin A alters permeability of the inner and outer membrane of Escherichia coli K-12
Curr Microbiol 1996 Jul;33(1):40-3.PMID:8661687DOI:10.1007/s002849900071.
Ceratotoxins are antibacterial 3-kDa amphiphilic peptides isolated from the female reproductive apparatus of the medfly Ceratitis capitata. The antibacterial activity of a chemically synthesized Ceratotoxin A (ctx A) has been investigated. Ctx A was mainly active against Gram-negative organisms, and it had a lytic effect on nongrowing Escherichia coli K-12. Data showed that ctx A alters both the outer and the inner membrane of E.coli K-12 cells.