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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 BRSV Fusion Glycoprotein, N-His
- 库存:
999
- 供应商:
abinScience
- 规格:
100ug

| Product name | Recombinant BRSV Fusion Glycoprotein, N-His |
|---|---|
| Catalog No. | VK027012 |
| 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 | P23728 |
| 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 | Fusion glycoprotein F0, Fusion glycoprotein F2, F2, p27, Intervening segment, Pep27, Peptide 27, Fusion glycoprotein F1, F1, F |
| Species | Bovine respiratory syncytial virus (strain Rb94) (BRS) |
| 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.
Main products...
Application field: Infectious disease research, Neuroscience, Immunology, Oncology
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文献和实验• The Hantavirus Surface Glycoprotein Lattice and Its Fusion Control Mechanism., PMID:32937107
• Lassa virus glycoprotein complex review: insights into its unique fusion machinery., PMID:35088070
• Structure, function, and evolution of the Orthobunyavirus membrane fusion glycoprotein., PMID:36827185
• Mapping glycoprotein structure reveals Flaviviridae evolutionary history., PMID:39232167
• Characterization of Galectin Fusion Proteins with Glycoprotein Affinity Columns and Binding Assays., PMID:36770718
• Endosomes supporting fusion mediated by vesicular stomatitis virus glycoprotein have distinctive motion and acidification., PMID:35147273
• Viral membrane fusion: is glycoprotein G of rhabdoviruses a representative of a new class of viral fusion proteins?, PMID:15933774
• Both chebulagic acid and punicalagin inhibit respiratory syncytial virus entry via multi-targeting glycoprotein and fusion protein., PMID:39508604
• Structural intermediates in the fusion-associated transition of vesiculovirus glycoprotein., PMID:28188244
Expression of Recombinant Proteins with Uniform N-Termini
Heterologously expressed proteins in Escherichia coli may undergo unwanted N-terminal processing by methionine and proline aminopeptidases. To overcome this problem, we present a system where the gene of interest is cloned as a fusion
The Use of Recombinant Fusion Proteases in the Affinity Purification of Recombinant Proteins
of interest, but some affinity tails are able to be linked to either the N- or C-terminus of the protein of interest. The choice of affinity tail to use for the expression of any particular protein is empirical since the factors leading to the high expression of recombinant
Fusion mediated by the human immunodeficiency virus type-1 (HIV-1) envelope (Env) glycoprotein and the cellular CD4/chemokine receptor complex is the first step in entry and is often analyzed in cell-cell fusion assays that require Env expression
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