199727-62-3|CEF3|CEF3|-范德生物科技公司

CEF3

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names：
CEF3
CAS号：
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)对应于甲型流感病毒M1蛋白的13-21个氨基酸序列。甲型流感病毒M1蛋白是一种多功能蛋白质，在病毒生命周期中起着重要的结构和功能作用。

货品编码	规格	纯度	价格 (¥)	现价(¥)	特价(¥)	库存描述	数量	总计 (¥)
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

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中文别名	CEF3(199727-62-3);SER-ILE-ILE-PRO-SER-GLY-PRO-LEU-LYS;
英文别名	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号	199727-62-3
SMILES	CCC(C)C(C(=O)NC(C(C)CC)C(=O)N1CCCC1C(=O)NC(CO)C(=O)NCC(=O)N2CCCC2C(=O)NC(CC(C)C)C(=O)NC(CCCCN)C(=O)O
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
闪点 FP	No data available
熔点 Melting point	No data available
沸点 Boiling point	No data available
Polarizability极化度
密度 Density	No data available
蒸汽压 Vapor Pressure
溶解度Solubility
性状	Solid
储藏条件 Storage conditions	请根据产品建议的存储条件进行存储,Please store the product under the recommended condition sin the description.

CEF3(199727-62-3,SIIPSGPLK)实验注意事项：
1.实验前需戴好防护眼镜，穿戴防护服和口罩，佩戴手套，避免与皮肤接触。
2.实验过程中如遇到有毒或者刺激性物质及有害物质产生，必要时实验操作需要手套箱内完成以免对实验人员造成伤害
3.实验后产生的废弃物需分类存储，并交于专业生物废气物处理公司处理，以免造成环境污染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试剂,CEF3杂质,CEF3中间体,CEF3密度,CEF3闪点,CEF3熔点,CEF3旋光度,CEF3溶解度,CEF3购买,CEF3 MSDS,

产品说明	CEF3(199727-62-3,SIIPSGPLK)对应于甲型流感病毒M1蛋白的13-21个氨基酸序列。
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蛋白是一种多功能蛋白质，在病毒生命周期中起着重要的结构和功能作用。
Application3

CEF3(199727-62-3,SIIPSGPLK)药理学：

1、甲型流感病毒的基质（M1）蛋白是一种多功能蛋白，在病毒的生命周期中起着至关重要的结构和功能作用。它驱动病毒出芽，是病毒体的主要蛋白质成分，在其中形成病毒包膜和整合膜蛋白与基因组核糖核蛋白（RNP）之间的中间层。它还有助于控制RNP的细胞内运输。这些作用主要是通过蛋白质与病毒以及可能与细胞蛋白质的相互作用来介导的。流感病毒M1是诱导vRNP核输出所必需的，但细胞磷酸化是另一个因素。流感病毒M1蛋白是病毒生命周期中晚期事件的基础-vRNP从细胞核转移到细胞质。

2、CEF3（SIIPSGPLK）对应于甲型流感病毒M1蛋白的aa 13-21。甲型流感病毒的基质（M1）蛋白是一种多功能蛋白，在病毒的生命周期中起着至关重要的结构和功能作用。

警示图
危险性	warning
危险性警示	Not available
安全声明	H303吞入可能有害+H313皮肤接触可能有害+H2413吸入可能对身体有害
安全防护	P264处理后彻底清洗+P280戴防护手套/穿防护服/戴防护眼罩/戴防护面具+P305如果进入眼睛+P351用水小心冲洗几分钟+P338取出隐形眼镜（如果有）并且易于操作,继续冲洗+P337如果眼睛刺激持续+P2393获得医疗建议/护理
备注	实验过程中防止吸入、食入，做好安全防护

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)参考文献：

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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