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核蛋白

NMR下載 COA and HPLC MSDS下載
names：
Nucleozin
CAS號：
341001-38-5
MDL Number： MFCD01426660
MF(分子式)： C21H19ClN4O4 MW(分子量)： 426.85
EINECS: Reaxys Number:
Pubchem ID:2863945 Brand:BIOFOUNT

核蛋白(341001-38-5,Nucleozin)核蛋白靶向流感A核蛋白（NP），這是病毒復制所必需的多功能，RNA結合蛋白。; IC50值：;目標：流感病毒NPNucleozin靶向流感A核蛋白，這是病毒復制所必需的多功能，RNA結合蛋白。它誘導核苷酸融合蛋白的形成并抑制其積累，從而干擾病毒復制。EC50在nM范圍內。核蛋白在H1N1，H3N2和H5N1流感病毒株中有效。

貨品編碼	規(guī)格	純度	價格 (￥)	現價(￥)	特價(￥)	庫存描述	數量	總計 (￥)
YZM000731-10mg	10mg	99.74%	￥ 911.00	￥ 911.00		2-3天	- +	￥ 0.00
YZM000731-5mg	5mg	99.74%	￥ 546.00	￥ 546.00		2-3天	- +	￥ 0.00

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中文別名	核蛋白(341001-38-5);1-（2-氯-4-硝基苯基）-4-[（5-甲基-3-苯基-4-異惡唑基）羰基]-哌嗪，核苷，[4-（2-氯-4-硝基苯基）-哌嗪-1-基]-（5-甲基-3-苯基-異惡唑-4-基）-甲酮;
英文別名	Nucleozin(341001-38-5);1-(2-Chloro-4-nitrophenyl)-4-[(5-methyl-3-phenyl-4-isoxazolyl)carbonyl]-piperazine, Nucleozin, [4-(2-Chloro-4-nitro-phenyl)-piperazin-1-yl]-(5-methyl-3-phenyl-isoxazol-4-yl)-methanone;
CAS號	341001-38-5
Inchi	InChI = 1S / C21H19ClN4O4 / c1-14-19（20（23-30-14）15-5-3-2-4-6-15）21（27）25-11-9-24（10-12- 25）18-8-7-16（26（28）29）13-17（18）22 / h2-8,13H，9-12H2,1H3
InchiKey	OWXBJAPOSQSWAO-UHFFFAOYSA-N
分子式 Formula	C21H19ClN4O4
分子量 Molecular Weight	426.85
溶解度Solubility	生物體外In Vitro:DMSO溶解度28.66 mg/mL(67.14 mM;Need ultrasonic)
性狀	黃色粉末,Power
儲藏條件 Storage conditions	2-8°C,-20°C 3 years年 4°C 2 years年 / In solvent溶液中:-80°C 6 months月 -20°C 1 month月

核蛋白(341001-38-5,Nucleozin)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(yè)生物廢氣物處理公司處理，以免造成環(huán)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.

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產品說明	核蛋白(341001-38-5,Nucleozin)是一種細胞可滲透的異惡唑基哌嗪,靶向流感A核蛋白(NP),可抑制AH1N1,H3N2和H5N1流感.
Introduction	核蛋白(341001-38-5,Nucleozin)targets influenza A nucleoprotein (NP), a multifunctional, RNAinding protein necessary for virus replication. IC50 Value:
Application1
Application2
Application3

核蛋白(341001-38-5,Nucleozin)藥理學：

核蛋白靶向流感A核蛋白（NP），這是病毒復制所必需的多功能，RNA結合蛋白。IC50值：目標：流感病毒NP核蛋白靶向流感A核蛋白，這是病毒復制所必需的多功能，RNA結合蛋白。它誘導核苷酸融合蛋白的形成并抑制其積累，從而干擾病毒復制。EC50在nM范圍內。核蛋白在H1N1，H3N2和H5N1流感病毒株中有效。

警示圖
危險性	warning
危險性警示	Acute Tox. 3
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(xù)沖洗+P337如果眼睛刺激持續(xù)+P2393獲得醫(yī)療建議/護理
備注	實驗過程中防止吸入、食入，做好安全防護

核蛋白(341001-38-5,Nucleozin)危害標識：

象形圖
信號	Danger
GHS危險說明	Aggregated GHS information provided by 38 companies from 1 notifications to the ECHA C&L Inventory.
	H301 (100%): Toxic if swallowed [Danger Acute toxicity, oral]
	Information may vary between notifications depending on impurities, additives, and other factors. The percentage value in parenthesis indicates the notified classification ratio from companies that provide hazard codes. Only hazard codes with percentage values above 10% are shown.
防范說明代碼	P264, P270, P301+P310, P321, P330, P405, and P501
防范說明代碼	(The corresponding statement to each P-code can be found at the GHS Classification page.)

Kao, Richard Y. et al. Identification of influenza A nucleoprotein as an antiviral target.Nature Biotechnology (2010), 28(6), 600-605.

Hung HC, Liu CL, Hsu JT, Horng JT, Fang MY, Wu SY, Ueng SH, Wang MY, Yaw CW, Hou MH.Development of an anti-influenza drug screening assay targeting nucleoproteins with tryptophan fluorescence quenchin

Su CY, Cheng TJ, Lin MI, Wang SY, Huang WI, Lin-Chu SY, Chen YH, Wu CY, Lai MM, Cheng WC, Wu YT, Tsai MD, Cheng YS, Wong CH.High-throughput identification of compounds targeting influenza RNA-dependen

Kao RY, Yang D, Lau LS, Tsui WH, Hu L, Dai J, Chan MP, Chan CM, Wang P, Zheng BJ, Sun J, Huang JD, Madar J, Chen G, Chen H, Guan Y, Yuen KY.Identification of influenza A nucleoprotein as an antiviral

核蛋白(341001-38-5,Nucleozin)參考文獻：

1.Development of an anti-influenza drug screening assay targeting nucleoproteins with tryptophan fluorescence quenching.
Hung HC;Liu CL;Hsu JT;Horng JT;Fang MY;Wu SY;Ueng SH;Wang MY;Yaw CW;Hou MH Anal Chem. 2012 Aug 7;84(15):6391-9. doi: 10.1021/ac2022426. Epub 2012 Jul 10.

Recent studies have shown that NP (nucleoprotein), which possesses multiple functions in the viral life cycle, is a new potential anti-influenza drug target. NP inhibitors reliably induce conformational changes in NPs, and these changes may confer inhibition of the influenza virus. The six conserved tryptophan residues in NP can be used as an intrinsic probe to monitor the change in fluorescence of the tryptophan residues in the protein upon binding to an NP inhibitor. In the present study, we found that the fluorescence of recombinant NP proteins was quenched following the binding of available NP inhibitors (such as nucleozin) in a concentration- and time-dependent manner, which suggests that the inhibitor induced conformational changes in the NPs. The minimal fluorescence-quenching effect and weak binding constant of nucleozin to the swine-origin influenza virus H1N1pdm09 (SOIV) NP revealed that the SOIV is resistant to nucleozin. We have used the fluorescence-quenching property of tryptophans in NPs that were bound to ligands in a 96-well-plate-based drug screen to assess the ability of promising small molecules to interact with NPs and have identified one new anti-influenza drug, CSV0C001018, with a high SI value.

2.E339...R416 salt bridge of nucleoprotein as a feasible target for influenza virus inhibitors.
Shen YF;Chen YH;Chu SY;Lin MI;Hsu HT;Wu PY;Wu CJ;Liu HW;Lin FY;Lin G;Hsu PH;Yang AS;Cheng YS;Wu YT;Wong CH;Tsai MD Proc Natl Acad Sci U S A. 2011 Oct 4;108(40):16515-20. doi: 10.1073/pnas.1113107108. Epub 2011 Sep 19.

The nucleoprotein (NP) of the influenza virus exists as trimers, and its tail-loop binding pocket has been suggested as a potential target for antiinfluenza therapeutics. The possibility of NP as a drug target was validated by the recent reports that nucleozin and its analogs can inhibit viral replication by inducing aggregation of NP trimers. However, these inhibitors were identified by random screening, and the binding site and inhibition mechanism are unclear. We report a rational approach to target influenza virus with a new mechanism--disruption of NP-NP interaction. Consistent with recent work, E339A, R416A, and deletion mutant Δ402-428 were unable to support viral replication in the absence of WT NP. However, only E339A and R416A could form hetero complex with WT NP, but the complex was unable to bind the RNA polymerase, leading to inhibition of viral replication. These results demonstrate the importance of the E339…R416 salt bridge in viral survival and establish the salt bridge as a sensitive antiinfluenza target. To provide further support, we showed that peptides encompassing R416 can disrupt NP-NP interaction and inhibit viral replication. Finally we performed virtual screening to target E339…R416, and some small molecules identified were shown to disrupt the formation of NP trimers and inhibit replication of WT and nucleozin-resistant strains.

3.Broad Spectrum Inhibitor of Influenza A and B Viruses Targeting the Viral Nucleoprotein.
White KM;Abreu P Jr;Wang H;De Jesus PD;Manicassamy B;García-Sastre A;Chanda SK;DeVita RJ;Shaw ML ACS Infect Dis. 2018 Feb 9;4(2):146-157. doi: 10.1021/acsinfecdis.7b00120. Epub 2018 Jan 4.

S119 was a top hit from an ultrahigh throughput screen performed to identify novel inhibitors of influenza virus replication. It showed a potent antiviral effect (50% inhibitory concentration, IC;50; = 20 nM) and no detectable cytotoxicity (50% cytotoxic concentration, CC;50; > 500 μM) to yield a selectivity index greater than 25?000. Upon investigation, we found that S119 selected for resistant viruses carrying mutations in the viral nucleoprotein (NP). These resistance mutations highlight a likely S119 binding site overlapping with but not identical to that found for the compound nucleozin. Mechanism of action studies revealed that S119 affects both the oligomerization state and cellular localization of the NP protein which has an impact on viral transcription, replication, and protein expression. Through a hit-to-lead structure-activity relationship (SAR) study, we found an analog of S119, named S119-8, which had increased breadth of inhibition against influenza A and B viruses accompanied by only a small loss in potency. Finally, in vitro viral inhibition assays showed a synergistic relationship between S119-8 and oseltamivir when they were combined, indicating the potential for future drug cocktails.

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