購物車 
-
CEF3
- names：
CEF3
- CAS號：
199727-62-3
MDL Number： - MF(分子式)： C42H74N10O12 MW(分子量)： 911.1
- EINECS: Reaxys Number:
- Pubchem ID:146157902 Brand:BIOFOUNT
CEF3(199727-62-3,SIIPSGPLK)對應于甲型流感病毒M1蛋白的13-21個氨基酸序列。甲型流感病毒M1蛋白是一種多功能蛋白質，在病毒生命周期中起著重要的結構和功能作用。
| 貨品編碼 | 規格 | 純度 | 價格 (￥) | 現價(￥) | 特價(￥) | 庫存描述 | 數量 | 總計 (￥) |
|---|---|---|---|---|---|---|---|---|
| YZM000750-5mg | 5mg | >97.0% | ￥ 4860.00 | ￥ 4860.00 | Backorder | ￥ 0.00 | ||
| YZM000750-1mg | 1mg | >97.0% | ￥ 1170.00 | ￥ 1170.00 | 2-3天 | ￥ 0.00 |
| 中文別名 | CEF3(199727-62-3);SER-ILE-ILE-PRO-SER-GLY-PRO-LEU-LYS; |
| 英文別名 | CEF3(199727-62-3);SIIPSGPLK;CEF3;INFLUENZA VIRUS M1 (13-21);H-SER-ILE-ILE-PRO-SER-GLY-PRO-LEU-LYS-OH;SER-ILE-ILE-PRO-SER-GLY-PRO-LEU-LYS;CEF3, Influenza Virus M1 (13-21); |
| CAS號 | 199727-62-3 |
| Inchi | InChI=1S/C42H74N10O12/c1-7-24(5)33(49-35(56)26(44)21-53)40(61)50-34(25(6)8-2)41(62)52-18-12-15-31(52)39(60)48-29(22-54)36(57)45-20-32(55)51-17-11-14-30(51)38(59)47-28(19-23(3)4)37(58)46-27(42(63)64)13-9-10-16-43/h23-31,33-34,53-54H,7-22,43-44H2,1-6H3,(H,45,57)(H,46,58)(H,47,59)(H,48,60)(H,49,56)(H,50,61)(H,63,64) |
| InchiKey | ZTJURUPAUNLCRP-UHFFFAOYSA-N |
| 分子式 Formula | C42H74N10O12 |
| 分子量 Molecular Weight | 911.1 |
| 溶解度Solubility | |
| 性狀 | Solid |
| 儲藏條件 Storage conditions | 請根據產品建議的存儲條件進行存儲,Please store the product under the recommended condition sin the description. |
CEF3(199727-62-3,SIIPSGPLK)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.
Tags：CEF3試劑,CEF3雜質,CEF3中間體,CEF3密度,CEF3閃點,CEF3熔點,CEF3旋光度,CEF3溶解度,CEF3購買,CEF3 MSDS,
| 產品說明 | CEF3(199727-62-3,SIIPSGPLK)對應于甲型流感病毒M1蛋白的13-21個氨基酸序列。 |
| Introduction | CEF3(199727-62-3,SIIPSGPLK)corresponds to aa 131 of the influenza A virus M1 protein. |
| Application1 | CEF3(199727-62-3,SIIPSGPLK)The matrix (M1) protein of influenza A virus is a multifunctional protein that plays essential structural and functional roles in the virus life cycle. |
| Application2 | CEF3(199727-62-3,SIIPSGPLK)中甲型流感病毒M1蛋白是一種多功能蛋白質，在病毒生命周期中起著重要的結構和功能作用。 |
| Application3 |
CEF3(199727-62-3,SIIPSGPLK)藥理學：
1、甲型流感病毒的基質（M1）蛋白是一種多功能蛋白，在病毒的生命周期中起著至關重要的結構和功能作用。它驅動病毒出芽，是病毒體的主要蛋白質成分，在其中形成病毒包膜和整合膜蛋白與基因組核糖核蛋白（RNP）之間的中間層。它還有助于控制RNP的細胞內運輸。這些作用主要是通過蛋白質與病毒以及可能與細胞蛋白質的相互作用來介導的。流感病毒M1是誘導vRNP核輸出所必需的，但細胞磷酸化是另一個因素。流感病毒M1蛋白是病毒生命周期中晚期事件的基礎-vRNP從細胞核轉移到細胞質。
2、CEF3（SIIPSGPLK）對應于甲型流感病毒M1蛋白的aa 13-21。甲型流感病毒的基質（M1）蛋白是一種多功能蛋白，在病毒的生命周期中起著至關重要的結構和功能作用。
| 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+H2413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+P2393獲得醫療建議/護理 |
| 備注 | 實驗過程中防止吸入、食入，做好安全防護 |
| Noton SL, et al. Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions. J Gen Virol. 2007 Aug;88(Pt 8):2280-9 |
| Bui M, et al. Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins. J Virol. 2000 Feb;74(4):1781-6. |
CEF3(199727-62-3,SIIPSGPLK)參考文獻：
1、Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins
M Bui 1, E G Wills, A Helenius, G R Whittaker
Abstract The protein kinase inhibitor H7 blocks influenza virus replication, inhibits production of the matrix protein (M1), and leads to a retention of the viral ribonucleoproteins (vRNPs) in the nucleus at late times of infection (K. Martin and A. Helenius, Cell 67:117-130, 1991). We show here that production of assembled vRNPs occurs normally in H7-treated cells, and we have used H7 as a biochemical tool to trap vRNPs in the nucleus. When H7 was removed from the cells, vRNP export was specifically induced in a CHO cell line stably expressing recombinant M1. Similarly, fusion of cells expressing recombinant M1 from a Semliki Forest virus vector allowed nuclear export of vRNPs. However, export was not rescued when H7 was present in the cells, implying an additional role for phosphorylation in this process. The viral NS2 protein was undetectable in these systems. We conclude that influenza virus M1 is required to induce vRNP nuclear export but that cellular phosphorylation is an additional factor.
2、Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions
Sarah L Noton 1, Elizabeth Medcalf, Dawn Fisher, Anne E Mullin, Debra Elton, Paul Digard
Abstract The matrix (M1) protein of influenza A virus is a multifunctional protein that plays essential structural and functional roles in the virus life cycle. It drives virus budding and is the major protein component of the virion, where it forms an intermediate layer between the viral envelope and integral membrane proteins and the genomic ribonucleoproteins (RNPs). It also helps to control the intracellular trafficking of RNPs. These roles are mediated primarily via protein-protein interactions with viral and possibly cellular proteins. Here, the regions of M1 involved in binding the viral RNPs and in mediating homo-oligomerization are identified. In vitro, by using recombinant proteins, it was found that the middle domain of M1 was responsible for binding NP and that this interaction did not require RNA. Similarly, only M1 polypeptides containing the middle domain were able to bind to RNP-M1 complexes isolated from purified virus. When M1 self-association was examined, all three domains of the protein participated in homo-oligomerization although, again, the middle domain was dominant and self-associated efficiently in the absence of the N- and C-terminal domains. However, when the individual fragments of M1 were tagged with green fluorescent protein and expressed in virus-infected cells, microscopy of filamentous particles showed that only full-length M1 was incorporated into budding virions. It is concluded that the middle domain of M1 is primarily responsible for binding NP and self-association, but that additional interactions are required for efficient incorporation of M1 into virus particles.
1、Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins
M Bui 1, E G Wills, A Helenius, G R Whittaker
Abstract The protein kinase inhibitor H7 blocks influenza virus replication, inhibits production of the matrix protein (M1), and leads to a retention of the viral ribonucleoproteins (vRNPs) in the nucleus at late times of infection (K. Martin and A. Helenius, Cell 67:117-130, 1991). We show here that production of assembled vRNPs occurs normally in H7-treated cells, and we have used H7 as a biochemical tool to trap vRNPs in the nucleus. When H7 was removed from the cells, vRNP export was specifically induced in a CHO cell line stably expressing recombinant M1. Similarly, fusion of cells expressing recombinant M1 from a Semliki Forest virus vector allowed nuclear export of vRNPs. However, export was not rescued when H7 was present in the cells, implying an additional role for phosphorylation in this process. The viral NS2 protein was undetectable in these systems. We conclude that influenza virus M1 is required to induce vRNP nuclear export but that cellular phosphorylation is an additional factor.
2、Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions
Sarah L Noton 1, Elizabeth Medcalf, Dawn Fisher, Anne E Mullin, Debra Elton, Paul Digard
Abstract The matrix (M1) protein of influenza A virus is a multifunctional protein that plays essential structural and functional roles in the virus life cycle. It drives virus budding and is the major protein component of the virion, where it forms an intermediate layer between the viral envelope and integral membrane proteins and the genomic ribonucleoproteins (RNPs). It also helps to control the intracellular trafficking of RNPs. These roles are mediated primarily via protein-protein interactions with viral and possibly cellular proteins. Here, the regions of M1 involved in binding the viral RNPs and in mediating homo-oligomerization are identified. In vitro, by using recombinant proteins, it was found that the middle domain of M1 was responsible for binding NP and that this interaction did not require RNA. Similarly, only M1 polypeptides containing the middle domain were able to bind to RNP-M1 complexes isolated from purified virus. When M1 self-association was examined, all three domains of the protein participated in homo-oligomerization although, again, the middle domain was dominant and self-associated efficiently in the absence of the N- and C-terminal domains. However, when the individual fragments of M1 were tagged with green fluorescent protein and expressed in virus-infected cells, microscopy of filamentous particles showed that only full-length M1 was incorporated into budding virions. It is concluded that the middle domain of M1 is primarily responsible for binding NP and self-association, but that additional interactions are required for efficient incorporation of M1 into virus particles.
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