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- 文献和实验
- 技术资料
- 保存条件:
Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
- 保质期:
1 year
- 英文名:
Recombinant Zebrafish mycl1a Protein, N-His-SUMO
- 库存:
999
- 供应商:
abinScience
- 规格:
50ug

| Product name | Recombinant Zebrafish mycl1a Protein, N-His-SUMO |
|---|---|
| Catalog No. | ZA436012 |
| Host species | Lyophilized |
| Specificity | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
| Conjugation | >90% as determined by SDS-PAGE. |
| Species reactivity | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Immunogen | Please contact with the lab for this information. |
| Form | E. coli |
| Storage buffer | Q9PSI9 |
| Purity | Ser286-Ser372 |
| Clonality | Recombinant |
| Isotype | 22.46 kDa |
| Applications | 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. |
| Target | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Purification | Protein L-Myc-1a, Protein L-Myc 1, zL-Myc, mycl1a |
| Accession | Danio rerio (Zebrafish) |
Abinscience, founded in 2023 and located in the innovation technology center in Strasbourg, France, is the core research reagent brand of ProteoGenix. Focusing on the development and production of life science research reagents, Abinscience takes "Empowering Bioscience Discovery" as its vision, and is committed to providing high-quality and innovative biological reagent products and technical solutions for global researchers.
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文献和实验tag by SUMO protease in vitro facilitates the generation of target protein with a native N-terminus. In addition to its physiological relevance in eukaryotes, SUMO can be used as a powerful biotechnology tool for enhanced functional protein expression
protein, the SUMO-tag can be cleaved by specific (SUMO) proteases via their endopeptidase activity in vitro to generate the desired N-terminus of the released protein partner. In addition to its physiological relevance in eukaryotes, SUMO
Strategies for the Expression of SUMO-Modified Target Proteins in Escherichia coli
We previously described the establishment of a binary vector system that allows co-expression of SUMO conjugation enzymes and a target protein of interest, leading to efficient SUMO modification and the production of a large
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