產品編號 |
bs-41491P |
英文名稱 |
Recombinant SARS-Cov-2 N protein (del204, del215), His
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中文名稱 |
重組SARS冠狀病毒核衣殼突變蛋白 (del204,del215) |
別 名 |
SARS-CoV-2 Nucleocapsid Protein; SARS-CoV-2 NP; nucleocapsid protein [Severe acute respiratory syndrome coronavirus 2]; novel coronavirus N Protein; novel coronavirus Nucleocapsid Protein; 2019-nCoV Nucleoprotein; 2019-nCoV N; 2019nCoV N; 2019-nCoV N Protein; 2019 ncov N Protein; 2019-nCoV nucleocapsid protein, 2019-nCOV Nucleocapsid protein (del204,del215),Recombinant (His Tag); Recombinant SARS-Cov-2 N protein (del204, del215), His 新冠病毒N蛋白; 新冠N蛋白; SARS-CoV-2 N蛋白; |
理論分子量 |
46kDa |
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 |
內毒素 |
Not analyzed |
表達系統(tǒng) |
E.coli |
活性 |
Not tested |
標簽 |
His |
緩 沖 液 |
20mM Tris-HCl (pH8.0). |
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.
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產品圖片 |
The purity of the protein is greater than 90% as determined by reducing SDS-PAGE.
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