購物車 
-
Α-毒傘肽
- names：
α-Amanitin
- CAS號：
23109-05-9
MDL Number： Not available - MF(分子式)： C39H54N10O14S MW(分子量)： 918.97
- EINECS:Not available Reaxys Number:Not available
- Pubchem ID:441541 Brand:BIOFOUNT
Α-毒傘肽(23109-05-9, α-Amanitin)是雙環八肽，屬于一大群原生質蘑菇毒素，被稱為阿托莫辛。Α-毒傘肽用于抗體-藥物結合（ADC）的細胞毒素中。Α-毒傘肽是幾種致命毒蘑菇的主要毒素，通過抑制 RNA聚合酶II 發揮其毒性作用。
| 貨品編碼 | 規格 | 純度 | 價格 (￥) | 現價(￥) | 特價(￥) | 庫存描述 | 數量 | 總計 (￥) |
|---|
| 中文別名 | Α-毒傘肽(23109-05-9, α-Amanitin),Α-鵝膏蕈堿,ALPHA-毒傘肽,alpha-鵝膏毒素 |
| 英文別名 | α-Amanitin(23109-05-9),alpha-amanitin,alpha-amanitine,α-Amatoxin |
| CAS號 | 23109-05-9 |
| Inchi | InChI=1S/C39H54N10O14S/c1-4-16(2)31-36(60)42-11-29(55)43-25-15-64(63)38-21(20-6-5-18(51)7-22(20)46-38)9-23(33(57)41-12-30(56)47-31)44-37(61)32(17(3)27(53)14-50)48-35(59)26-8-19(52)13-49(26)39(62)24(10-28(40)54)45-34(25)58/h5-7,16-17,19,23-27,31-32,46,50-53H,4,8-15H2,1-3H3,(H2,40,54)(H,41,57)(H,42,60)(H,43,55)(H,44,61)(H,45,58)(H,47,56)(H,48,59)/t16-,17-,19+,23-,24-,25-,26-,27-,31-,32-,64+/m0/s1 |
| InchiKey | CIORWBWIBBPXCG-SXZCQOKQSA-N |
| 分子式 Formula | C39H54N10O14S |
| 分子量 Molecular Weight | 918.97 |
| 溶解度Solubility | |
| 性狀 | 淺黃色至黃色固體粉末 |
| 儲藏條件 Storage conditions | Powder -20°C 3 years （該產品在溶液狀態不穩定，建議您現用現配，即刻使用） |
Α-毒傘肽(23109-05-9, α-Amanitin)實驗注意事項：
1.實驗前需戴好防護眼鏡，穿戴防護服和口罩，佩戴手套，避免與皮膚接觸。
2.實驗過程中如遇到有毒或者刺激性物質及有害物質產生，必要時實驗操作需要手套箱內完成以免對實驗人員造成傷害
3.實驗后產生的廢棄物需分類存儲，并交于專業生物廢氣物處理公司處理，以免造成環境污染
α-Amanitin(23109-05-9) Experimental considerations:
1. Wear protective glasses, protective clothing and masks, gloves, and avoid contact with the skin during the experiment.
2. The waste generated after the experiment needs to be stored separately, and handed over to a professional biological waste gas treatment company to avoid environmental pollution.
Tag:Α-毒傘肽(23109-05-9, α-Amanitin),Α-毒傘肽試劑,Α-毒傘肽抑制劑,Α-毒傘肽雜質,Α-毒傘肽的作用,Α-毒傘肽的純度,Α-毒傘肽的外觀,Α-毒傘肽的使用,Α-毒傘肽的外觀,Α-毒傘肽的含量
| 產品說明 | Α-毒傘肽(23109-05-9, α-Amanitin)是幾種致命毒蘑菇的主要毒素，23109-05-9通過抑制RNA聚合酶II發揮毒性作用 |
| Introduction | α-Amanitin(23109-05-9,Α-毒傘肽) is the main toxin of several deadly poisonous mushrooms, and exerts its toxic effect by inhibiting RNA polymerase II. |
| Application1 | α-Amanitin is a bicyclic octapeptide which belongs to a large group of protoplasmic mushroom toxins known as amatoxins. α-Amanitin is used in a cytotoxin in antibody-drug-conjugation (ADC). |
| Application2 | |
| Application3 |
RNA and protein synthesis is required for Ancylostoma caninum larval activation.
Dryanovski DI;Dowling C;Gelmedin V;Hawdon JM Vet Parasitol. 2011 Jun 30;179(1-3):137-43. doi: 10.1016/j.vetpar.2011.01.062. Epub 2011 Feb 26.
The developmentally arrested infective larva of hookworms encounters a host-specific signal during invasion that initiates the resumption of suspended developmental pathways. The resumption of development during infection is analogous to recovery from the facultative arrested dauer stage in the free-living nematode Caenorhabditis elegans. Infective larvae of the canine hookworm Ancylostoma caninum resume feeding and secrete molecules important for infection when exposed to a host mimicking signal in vitro. This activation process is a model for the initial steps of the infective process. Dauer recovery requires protein synthesis, but not RNA synthesis in C. elegans. To determine the role of RNA and protein synthesis in hookworm infection, inhibitors of RNA and protein synthesis were tested for their effect on feeding and secretion by A. caninum infective larvae. The RNA synthesis inhibitors α-amanitin and actinomycin D inhibit feeding dose-dependently, with IC(50) values of 30 and 8 μM, respectively. The protein synthesis inhibitors puromycin (IC(50)=110 μM), cycloheximide (IC(50)=50 μM), and anisomycin (IC(50)=200 μM) also displayed dose-dependent inhibition of larval feeding. Significant inhibition of feeding by α-amanitin and anisomycin occurred when the inhibitors were added before 12h of the activation process, but not if the inhibitors were added after 12h.
Dryanovski DI;Dowling C;Gelmedin V;Hawdon JM Vet Parasitol. 2011 Jun 30;179(1-3):137-43. doi: 10.1016/j.vetpar.2011.01.062. Epub 2011 Feb 26.
The developmentally arrested infective larva of hookworms encounters a host-specific signal during invasion that initiates the resumption of suspended developmental pathways. The resumption of development during infection is analogous to recovery from the facultative arrested dauer stage in the free-living nematode Caenorhabditis elegans. Infective larvae of the canine hookworm Ancylostoma caninum resume feeding and secrete molecules important for infection when exposed to a host mimicking signal in vitro. This activation process is a model for the initial steps of the infective process. Dauer recovery requires protein synthesis, but not RNA synthesis in C. elegans. To determine the role of RNA and protein synthesis in hookworm infection, inhibitors of RNA and protein synthesis were tested for their effect on feeding and secretion by A. caninum infective larvae. The RNA synthesis inhibitors α-amanitin and actinomycin D inhibit feeding dose-dependently, with IC(50) values of 30 and 8 μM, respectively. The protein synthesis inhibitors puromycin (IC(50)=110 μM), cycloheximide (IC(50)=50 μM), and anisomycin (IC(50)=200 μM) also displayed dose-dependent inhibition of larval feeding. Significant inhibition of feeding by α-amanitin and anisomycin occurred when the inhibitors were added before 12h of the activation process, but not if the inhibitors were added after 12h.
| 警示圖 | |
| 危險性 | warning |
| 危險性警示 | Not available |
| 安全聲明 | H303吞入可能有害+H313皮膚接觸可能有害+H333吸入可能對身體有害 |
| 安全防護 | P264處理后徹底清洗+P280戴防護手套/穿防護服/戴防護眼罩/戴防護面具+P305如果進入眼睛+P351用水小心沖洗幾分鐘+P338取出隱形眼鏡（如果有）并且易于操作,繼續沖洗+P337如果眼睛刺激持續+P313獲得醫療建議/護理 |
| 備注 | α-AmanitinCURRENTLY UNAVAILABLE實驗過程中防止吸入、食入，做好安全防護 |
| A Convergent Total Synthesis of the Death Cap Toxin α-Amanitin |
| In vitro mechanistic studies on α-amanitin and its putative antidotes |
| Highly sensitive α-amanitin sensor based on molecularly imprinted photonic crystals |
Lamin A/C speckles mediate spatial organization of splicing factor compartments and RNA polymerase II transcription.
Kumaran RI;Muralikrishna B;Parnaik VK J Cell Biol. 2002 Dec 9;159(5):783-93. Epub 2002 Dec 9.
The A-type lamins have been observed to colocalize with RNA splicing factors in speckles within the nucleus, in addition to their typical distribution at the nuclear periphery. To understand the functions of lamin speckles, the effects of transcriptional inhibitors known to modify RNA splicing factor compartments (SFCs) were examined. Treatment of HeLa cells with alpha-amanitin or 5,6-dichlorobenzimidazole riboside (DRB) inhibited RNA polymerase II (pol II) transcription and led to the enlargement of lamin speckles as well as SFCs. Removal of the reversible inhibitor DRB resulted in the reactivation of transcription and a rapid, synchronous redistribution of lamins and splicing factors to normal-sized speckles, indicating a close association between lamin speckles and SFCs. Conversely, the expression of NH2-terminally modified lamin A or C in HeLa cells brought about a loss of lamin speckles, depletion of SFCs, and down-regulation of pol II transcription without affecting the peripheral lamina. Our results suggest a unique role for lamin speckles in the spatial organization of RNA splicing factors and pol II transcription in the nucleus.
Kumaran RI;Muralikrishna B;Parnaik VK J Cell Biol. 2002 Dec 9;159(5):783-93. Epub 2002 Dec 9.
The A-type lamins have been observed to colocalize with RNA splicing factors in speckles within the nucleus, in addition to their typical distribution at the nuclear periphery. To understand the functions of lamin speckles, the effects of transcriptional inhibitors known to modify RNA splicing factor compartments (SFCs) were examined. Treatment of HeLa cells with alpha-amanitin or 5,6-dichlorobenzimidazole riboside (DRB) inhibited RNA polymerase II (pol II) transcription and led to the enlargement of lamin speckles as well as SFCs. Removal of the reversible inhibitor DRB resulted in the reactivation of transcription and a rapid, synchronous redistribution of lamins and splicing factors to normal-sized speckles, indicating a close association between lamin speckles and SFCs. Conversely, the expression of NH2-terminally modified lamin A or C in HeLa cells brought about a loss of lamin speckles, depletion of SFCs, and down-regulation of pol II transcription without affecting the peripheral lamina. Our results suggest a unique role for lamin speckles in the spatial organization of RNA splicing factors and pol II transcription in the nucleus.
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