Catalog NO.:BE7003
Applications :WB
Reactivity :ALL
货号 | 规格 | 品牌 | 库存 | 价格 | 数量 | 操作 |
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BE7003-100 | 100ul/支 | EASYBIO |
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The DYKDDDDK peptide (Flag-tag) is a small component of an epitope which does not appear to interfere with the bioactivity or the biodistribution of the recombinant protein. It has been used extensively as a general epitope tag in expression vectors. It can be used for affinity chromatography, then used to separate recombinant, overexpressed protein from wild-type protein expressed by the host organism. It can also be used in the isolation of protein complexes with multiple subunits.A Flag-tag can be used in many different assays that require recognition by an antibody. If there is no antibody against the studied protein, adding a Flag-tag to this protein allows one to follow the protein with an antibody against the Flag sequence.
Product Name: | flag-HRP Mouse Monoclonal Antibody |
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Isotype: | IgG1 |
Storage Buffer : | PBS, pH 7.4, containing 0.02% kathon as Preservative and 50% Glycerol |
Storage instructions: | -20°C. Do not aliquot the antibody |
Recommended dilutions: | WB: 1:2,000-5,000 |
Optimal dilutions should be determined by the end user. | |
Specificity: | The Flag tag antibody can recognize C-terminal, internal, and N-terminal Flag-tag fusion proteins. |
Alternative Names: | DDDDK epitope tag, DYKDDDDK epitope tag, ECS epitope tag |
Form: | Liquid |
Reactivity: | ALL |
[2]Huang, J., Zhao, Y., Liu, S., Chen, Y., Du, M., Wang, Q., Zhang, J., Yang, X., Chen, J., & Zhang, X. (2024). RH20, a phase-separated RNA helicase protein, facilitates plant resistance to viruses. Plant science : an international journal of experimental plant biology, 347, 112176. https://doi.org/10.1016/j.plantsci.2024.112176
[3]Huang, J., Du, J., Liu, Y., Lu, L., Xu, Y., Shi, J., Liu, Q., Li, Q., Liu, Y., Chen, Y., Du, M., Zhao, Y., Huo, L., Wang, W., Ding, C., Wei, L., Wu, J., Yuan, Y. W., Chen, J., Li, R., … Zhang, X. (2025). RH3 enhances antiviral defense by facilitating small RNA loading into Argonaute 2 at endoplasmic reticulum-chloroplast membrane contact sites. Nature communications, 16(1), 1953. https://doi.org/10.1038/s41467-025-57296-6