Recombinant Human ARPP19 Prote
in (N-His-SUMO & C-Strep Tag), 重组人ARPP19蛋白 (N端His-SUMO标签 & C端Strep标签)- ￥1268
- abinscience
- France
- HX213012
- 2026年03月03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 20 mM Tris-HCl pH 8.0, 100 mM NaCl,1mM EDTA, 4%trehalose,3402% mannitol.
- 保质期：
1 year
- 英文名：
Recombinant Human ARPP19 Protein, N-His-SUMO & C-Strep
- 库存：
999
- 供应商：
abinscience
- 规格：
50ug
| Product name | Recombinant Human ARPP19 Protein, N-His-SUMO & C-Strep |
|---|---|
| Catalog No. | HX213012 |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM 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 | P56211 |
| Protein length | Ser2-Leu77 |
| Nature | Recombinant |
| Predicted molecular weight | 22.08 kDa |
| Stability and Storage | 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. |
| Alternative Names | cAMP-regulated phosphoprotein 19, ARPP19, ARPP-19 |
| Species | Homo sapiens (Human) |
| Note | For research use only. |
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-His-Pro-Gln-Phe-Glu-Lys) 可放在N- 或 C-terminus 不影响蛋白折叠和功能，无需移除 分子量 1058Da Twin-Strep-tag® （也有叫做双Strep-tag®II） 28 aa 标签(WSHPQFEK-GGGSGGGSGG-SA-WSHPQFEK) 两段Strep-tag®II标签序列 较Strep-tag®II对于Strep-Tactin®有更高亲和力 分子量 2887Da 二者均为小标签，不会对蛋白质的结构和功能活性产生影响，因此通常不需要在纯化
depends on product and its function. N-terminal sequencing revealed that the purified rBoNTC(Hc )-N is missing the first eight amino acids of the N-terminus of the protein, whereas the purified rBoNTC(Hc )-C protein is intact. After a mouse bioassay test
N-Linked Protein Glycosylation in a Bacterial System
and permethylation followed by mass spectrometry. We also describe the expression and immunodetection of the model N -glycoprotein, AcrA, fused to a hexa-histidine tag to follow protein glycosylation in C. jejuni . This chapter concludes with the recent demonstration
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