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Mouse Anti-H1N1 nucleoprotein/Cy5 Conjugated antibody (bs-4971M-Cy5)
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說(shuō) 明 書(shū): 100ul  
100ul/2980.00元
大包裝/詢(xún)價(jià)
產(chǎn)品編號(hào) bs-4971M-Cy5
英文名稱(chēng)1 Mouse Anti-H1N1 nucleoprotein/Cy5 Conjugated antibody
中文名稱(chēng) Cy5標(biāo)記的鼠抗人禽流感A核蛋白抗體
別    名 Nucleoprotein; Nucleocapsid protein; Protein N; Influenza A virus H1N1; H3N2 nucleoprotein; H9N2 nucleoprotein; H2N2 nucleoprotein; H3N8 nucleoprotein; H7N7 nucleoprotein; H5N1 nucleoprotein.  
規(guī)格價(jià)格 100ul/2980元 購(gòu)買(mǎi)        大包裝/詢(xún)價(jià)
說(shuō) 明 書(shū) 100ul  
研究領(lǐng)域 細(xì)胞生物  免疫學(xué)  細(xì)菌及病毒  
抗體來(lái)源 Mouse
克隆類(lèi)型 Monoclonal
交叉反應(yīng)
產(chǎn)品應(yīng)用
not yet tested in other applications.
optimal dilutions/concentrations should be determined by the end user.
分 子 量 55-58kDa
性    狀 Lyophilized or Liquid
濃    度 1mg/ml
免 疫 原 KLH conjugated synthetic peptide derived from Influenza A virus H1N1 nucleoprotein
亞    型 IgG
純化方法 affinity purified by Protein A
儲(chǔ) 存 液 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
保存條件 Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.
產(chǎn)品介紹 background:
Influenza A virus is a major public health threat. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. There was some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species jumping ability.

Function:
Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals and is responsible of the active RNP import into the nucleus through the cellular importin alpha/beta pathway. Later in the infection, nucleus export of RNP are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that the nucleoprotein binds directly exportin-1 (XPO1) and plays an active role in RNP nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmask nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.

Subunit:
Homomultimerizes to form the nucleocapsid. May bind human exportin-1. Binds to viral genomic RNA. Protein-RNA contacts are mediated by a combination of electrostatic interactions between positively charged residues and the phosphate backbone and planar interactions between aromatic side chains and bases.

Subcellular Location:
Virion (Potential). Host nucleus.

Similarity:
Belongs to the influenza viruses nucleoprotein family.

Database links:
UniProtKB/Swiss-Prot: B4URE0.1

Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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