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Recombinant SARS-COV-2 Spike RBD(Omicron XBB) Protein, His Tag
- 品牌:翌圣生物
- 产地:
- 供应商报价:面议
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翌圣生物科技(上海)股份有限公司
更新时间:2024-12-24 09:03:45
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详细介绍
Coronaviruses are commonly comprised of four structural proteins: Spike protein (S), Envelope protein (E), Membrane protein (M) and Nucleocapsid protein (N) . The SARS-CoV-2 S protein is a glycoprotein that mediates membrane fusion and viral entry. The S protein is homotrimeric, with each ~180-kDa monomer consisting of two subunits, S1 and S2 . The RBD of SARS-CoV-2 binds a metallopeptidase, angiotensin-converting enzyme 2 (ACE-2).
产品信息
别名
S protein RBD; S glycoprotein RBD; Spike protein RBD
Accession
QHD43416.1
表达区间及表达系统
Recombinant SARS-CoV-2 Spike RBD (Omicron XBB) Protein is expressed from Expi293 with His tag at the C-terminal. It contains Arg319-Phe541(G339H, R346T, L368I, S371F, S373P, S375F, T376A, D405N, R408S, K417N, N440K, V445P, G446S, N460K, S477N, T478K, E484A, F486S, F490S, Q498R, N501Y, Y505H).
分子量
Approximately 26.21 kDa. Due to glycosylation, the protein migrates to 35-45 kDa based on Tris-Bis PAGE result.
纯度
> 95% as determined by SDS-PAGE and HPLC.
活性
ELISA Data:Immobilized SARS-CoV-2 Spike RBD (Omicron XBB) at 0.5μg/ml (100μl/well) on the plate. Dose response curve for Human ACE2, hFc Tag with the EC50 of 27.0ng/ml determined by ELISA.
内毒素
< 1.0 EU per 1μg of the protein by the LAL method.
制剂
Lyophilized from 0.22μm filtered solution in PBS (pH 7.4).
复溶
Centrifuge tubes before opening. Reconstituting to a concentration more than 100 μg/mL is recommended (usually we use 1 mg/mL solution for lyophilization). Dissolve the lyophilized protein in distilled water.
储存条件
The product should be stored at -25~-15℃.
1 month, 2 ~8 °C under sterile conditions after reconstitution.
3 months, -25~-15℃ °C under sterile conditions after reconstitution.
Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.
注意事项
1.Please operate with lab coats and disposable gloves,for your safety。
2.This product is for research use only.
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