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- 详细信息
- 文献和实验
- 技术资料
- 保存条件:
Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
- 保质期:
1 year
- 英文名:
Recombinant FMDV Protease 3C Protein, N-His
- 供应商:
abinScience
- 规格:
50ug/100ug/1mg

| Product name | Recombinant FMDV Protease 3C Protein, N-His |
|---|---|
| Catalog No. | VK500112 |
| 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 |
| Target | / |
| Expression system | E. coli |
| Accession | P03307 |
| Protein length | Ser1650-Glu1862 |
| Alternative Names | Genome polyprotein, Leader protease, Lpro, EC:3.4.22.46, Capsid protein VP0, VP4-VP2, Capsid protein VP4, P1A, Virion protein 4, Capsid protein VP2, P1B, Virion protein 2, Capsid protein VP3, P1C, Virion protein 3, Capsid protein VP1, P1D, Virion protein 1, Protein 2A, P2A, P52, Protein 2B, P2B, Protein 2C, P2C, EC:3.6.1.15, Protein 3A, P3A, Protein 3B-1, P3B-1, Genome-linked protein VPg1, Protein 3B-2, P3B-2, Genome-linked protein VPg2, Protein 3B-3, P3B-3, Genome-linked protein VPg3, Protease 3C, EC:3.4.22.28, Picornain 3C, P3C, Protease P20B, RNA-directed RNA polymerase 3D-POL, P3D-POL, EC:2.7.7.48, P56A |
| Predicted molecular weight | 25.32 kDa |
| Applications.1 | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Protein length.1 | Ser1650-Glu1862 |
| Species | Foot-and-mouth disease virus (isolate -/Germany/A5Westerwald/1951 serotype A) (FMDV) |
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, abinScience has inherited advanced technologies and high-quality standards. In particular, the XtenCHO™ system developed by ProteoGenix, which has two modes of transient expression and stable expression, has been widely recognized as a core technology to improve the efficiency of protein production, providing a solid foundation for ab...
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Application field
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Neuroscience research: Supporting research on neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease.
Immunology research: Covers the research needs of immune activation, inhibition, and allergies and abnormal reactions.
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文献和实验• Impact of VP2 structure on antigenicity: comparison of BTV1 and the highly virulent BTV8 serotype., PMID:39320096
• Identification of Potential Novel B-Cell Epitopes of Capsid Protein VP2 in Senecavirus A., PMID:37428080
• Conserved Rotavirus NSP5 and VP2 Domains Interact and Affect Viroplasm., PMID:31915278
• Neddylation of Enterovirus 71 VP2 Protein Reduces Its Stability and Restricts Viral Replication., PMID:35510863
• Sialic Acid Binding Sites in VP2 of Bluetongue Virus and Their Use during Virus Entry., PMID:34669428
• A potential dual protection vaccine: Recombinant feline herpesvirus-1 expressing feline parvovirus VP2 antigen., PMID:38185071
• Production of infectious reporter murine norovirus by VP2 trans-complementation., PMID:38226813
• Interaction between the VP2 protein of deformed wing virus and host snapin protein and its effect on viral replication., PMID:36846748
• Preparation and immunogenicity studies of NvIBDV VP2-ferritin nanoparticles., PMID:40764574
, and usually final protein yield between 0.1 and 2 mg/g cells is acceptable. Another concern is protein degradation. Especially with Pichia , protease activity during cell lysis and purification is always an issue. The importance of N-terminal degradation
Expression and Purification of Hepatitis C Virus Protease from Clinical Samples
This chapter describes the procedures for production of recombinant hepatitis C virus (HCV) NS3 protease from clinical samples, which can be used in the biochemical assays to assess the impact of different drug-resistant mutations in the NS
Proteome-wide analysis of protein C-termini has long been inaccessible, but is now enabled by a newly developed negative selection strategy we term C-terminomics. In this procedure, amine- and carboxyl groups of full-length proteins
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