- ￥1868
- abinScience
- France
- VK025012
- 2025年08月14日
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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 Avian myelocytomatosis virus MYC Protein, N-His-KSI
- 库存：
999
- 供应商：
abinScience
- 规格：
100ug
| Product name | Recombinant Avian myelocytomatosis virus MYC Protein, N-His-KSI |
|---|---|
| Catalog No. | VK025012 |
| 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 | P10395 |
| 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 | Viral myc transforming protein, v-Myc, MYC |
| Species | Avian myelocytomatosis virus 29 |
| 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• TRIM21 induces selective autophagic degradation of c-Myc and sensitizes regorafenib therapy in colorectal cancer., PMID:39388269
• Association of gag-myc proteins from avian myelocytomatosis virus wild-type and mutants with chromatin., PMID:6329716
• Isolation and characterization of c-myc, a cellular homolog of the oncogene (v-myc) of avian myelocytomatosis virus strain 29., PMID:6284994
• Identification and nucleotide sequence of a human locus homologous to the v-myc oncogene of avian myelocytomatosis virus MC29., PMID:6298632
• Nucleotide sequence analysis of human c-myc locus, chicken homologue, and myelocytomatosis virus MC29 transforming gene reveals a highly conserved gene product., PMID:6304729
• Site-directed mutagenesis of the gag-myc gene of avian myelocytomatosis virus 29: biological activity and intracellular localization of structurally altered proteins., PMID:3018283
• B-Cell Metabolic Remodeling and Cancer., PMID:29458963
• Cloning and characterization of different human sequences related to the onc gene (v-myc) of avian myelocytomatosis virus (MC29)., PMID:6292905
• Nucleotide sequence analysis of the chicken c-myc gene reveals homologous and unique coding regions by comparison with the transforming gene of avian myelocytomatosis virus MC29, delta gag-myc., PMID:6300896
Sequences derived from the respiratory syncytial virus (RSV) fusion (F) protein were expressed in insect cells as recombinant glutathione-S -transferase (GST)-tagged proteins. The sequence covering the F2 subunit (GST-F2), and a truncated
Quality Assessment of Recombinant Proteins Produced in Plants
Plant-based expression technologies for recombinant proteins have begun to receive acceptance for pharmaceuticals and other commercial markets. Protein products derived from plants offer safer, more cost-effective, and less capital-intensive
In-Fusion Cloning with Vaccinia Virus DNA Polymerase
the complementary ends and promotes joint molecule formation. Vaccinia virus single-stranded DNA binding protein can be added to enhance this reaction, although it is not an essential component. The resulting joint molecules are used to transform E. coli
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