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Recombinant SARS-Cov-2 (Omicron, B.1.1.529) N protein (P13L, E31del, R32del, S33del, R203K, G204R), N-His (bs-41494P)  
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說明書: 100ug  500ug  
100ug/5980.00元
500ug/16800.00元
大包裝/詢價

產(chǎn)品編號 bs-41494P
英文名稱 Recombinant SARS-Cov-2 (Omicron, B.1.1.529) N protein (P13L, E31del, R32del, S33del, R203K, G204R), N-His
中文名稱 重組SARS冠狀病毒2核衣殼突變體蛋白Omicron(P13L、E31del、R32del、S33del、R203K、G204R)
別    名 Recombinant SARS-Cov-2 (Omicron, B.1.1.529) N protein (P13L, E31del, R32del, S33del, R203K, G204R), N-His  
理論分子量 45.3kDa
檢測分子量 50
性    狀 Lyophilized or Liquid
濃    度 >0.5 mg/ml
物    種 SARS-Cov-2
序    列 1-419/419
純    度 >90% as determined by SDS-PAGE
純化方法 AC
內(nèi)毒素 Not analyzed
表達系統(tǒng) E.coli
活性 Not tested
標(biāo)簽 N-His
緩 沖 液 10mM PB (pH7.4) with 50mM NaCl.
保存條件 Stored at -70℃ or -20℃. Avoid repeated freeze/thaw cycles.
注意事項 This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
產(chǎn)品介紹 Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. Coronavirus N protein is required for coronavirus RNA synthesis, and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is a most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.

SWISS:
P0DTC9

Gene ID:
43740575

產(chǎn)品圖片
The purity of the protein is greater than 90% as determined by reducing SDS-PAGE.
The purity of the protein is greater than 90% as determined by reducing SDS-PAGE.
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