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Recombinant SARS-Cov-2 N protein, C-His (bs-41442P)
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產(chǎn)品編號(hào) bs-41442P
英文名稱 Recombinant SARS-Cov-2 N protein, C-His
中文名稱 重組SARS冠狀病毒2核衣殼蛋白
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. ;Recombinant SARS-Cov-2 N protein, 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(cè)分子量 50 kDa
性    狀 Lyophilized or Liquid
濃    度 >0.5 mg/ml
物    種 SARS-Cov-2
序    列 1-419/419
純    度 >95% as determined by SDS-PAGE
純化方法 AC
內(nèi)毒素 Not analyzed
表達(dá)系統(tǒng) E.coli
活性 Not tested
標(biāo)簽 C-His
緩 沖 液 20 mM Tris-HCl (pH=8.0) with 500 mM NaCl
保存條件 Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.
注意事項(xiàng) 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.
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