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- 详细信息
- 文献和实验
- 技术资料
- 保存条件:
Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.
- 保质期:
1 year
- 英文名:
Recombinant Human ATP5F1E Protein, N-His-KSI
- 库存:
999
- 供应商:
abinScience
- 规格:
100ug

| Product name | Recombinant Human ATP5F1E Protein, N-His-KSI |
|---|---|
| Catalog No. | HB493012 |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. |
| Purity | >90% as determined by SDS-PAGE. |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Endotoxin level | Please contact with the lab for this information. |
| Expression system | E. coli |
| Accession | P56381 |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Alternative Names | ATP synthase subunit epsilon, mitochondrial; ATPase subunit epsilon; ATP synthase F1 subunit epsilon; ATP5F1E; ATP5E |
| Species | Homo sapiens (Human) |
| Shipping | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
abinScience, founded in 2023 in Strasbourg, France, is committed to developing and producing high-quality life science reagents. Rooted in one of Europe’s leading hubs for scientific innovation, abinScience empowers global research through reliable, efficient experimental solutions. Guided by the vision of “Empowering Bioscience Discovery,” we support scientists worldwide in advancing the frontiers of bioscience.
Technology and Innovation
Relying on the global leading position in antibody and protein research and more than 20 years of industry experience of its parent company ProteoGenix since 2003...
Product categories and application fields.
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Application field: Infectious disease research, Neuroscience, Immunology, Oncology
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Medium-Throughput Production of Recombinant Human Proteins: Protein Production in E. coli
In Chapter 4 we described the SGC process for generating multiple constructs of truncated versions of each protein using LIC. In this chapter we provide a step-by-step procedure of our E . coli system for test expressing intracellular
Resolving Bottlenecks for Recombinant Protein Expression in E. coli
regarding expression of recombinant proteins in E. coli . However, despite this progress, protein production, primarily of eukaryotic origin, still remains a challenge. The biggest obstacle lies in obtaining large amounts of a given protein in a correctly
Expression of Recombinant Proteins with Uniform N-Termini
to a self-splicing mini-intein. This fusion construct is expressed in an engineered E. coli strain from which the pepP gene coding for aminopeptidase P has been deleted. We describe a protocol using human cationic trypsinogen as an example to demonstrate
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