Recombinant H4N6 (A/Swine/Ontario/01911-1/99) HA Protein (His Tag) | 重组甲型流感 H4N6 (A/Swine/Ontario/01911-1/99) HA 蛋白 (His标签)
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- Sino Biological
- 北京
- 11706-V08H
- 2025年08月12日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
在-20℃ to -80℃
- 保质期：
12个月
- 英文名：
Recombinant H4N6 (A/Swine/Ontario/01911-1/99) HA Protein (His Tag)
- 库存：
99
- 供应商：
北京义翘神州科技股份有限公司
- 规格：
100 µg
蛋白名称：Hemagglutinin/HA蛋白, Hemagglutinin/HA protein
蛋白构建：A DNA sequence encoding the extracellular domain (Met 1-Ile 528) of the influenza A hemagglutinin (A/Swine/Ontario/01911-1/99 (H4N6)) (AAG17429.1) (HA1+HA2, uncleaved) was expressed, fused with a C-terminal polyhistidine tag.
表达宿主：HEK293 Cells
蛋白纯度：> 92 % as determined by SDS-PAGE
蛋白活性：0
蛋白内毒素：< 1.0 EU per μg of the protein as determined by the LAL method
预测N端：Gln 17
蛋白分子量：The secreted recombinant influenza A H4N6 HA (A/Swine/Ontario/01911-1/99 (H4N6)) comprises 523 amino acids and has a predicted molecular mass of 59 kDa. As a result of glycosylation, it migrates as an approximately 65-75 kDa band in SDS-PAGE under reducing conditions.
蛋白NP号：AAG17429.1
蛋白氨基酸序列：Met1-Ile528
蛋白标签：C-His
蛋白保存条件：Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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文献和实验Recombinant DNA Engineering, Or Cloning Genes In Plasmids
and thus fusion proteins. For example there might be sequence for a fluorescent protein such as GFP or a peptide tag such as HA upstream of MCS (and downstream of promoter) so that an insert in frame will lead to the generation of a fusion protein, an N-terminal
of complex and protein alone with the naked eye or a light microscope, crystals of covalently Cy5?labeled DNA can be directly used for X?ray diffraction data collection. Curr. Protoc. Nucleic Acid Chem. 46:7.15.1?7.15.8. © 2011 by John Wiley & Sons
Purifying the Hedgehog Protein and its Variants
The purification of recombinant versions of the N-terminal signaling fragment of Sonic hedgehog (ShhN) from E. coli , Hi-5™ insect cells, yeast, and mammalian cell sources reveals diverse post-translational modifications that affect
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