Code | CSB-YP352404IFY |
MSDS | |
Size | Pls inquire |
Source | Yeast |
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Code | CSB-EP352404IFY |
MSDS | |
Size | Pls inquire |
Source | E.coli |
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Code | CSB-EP352404IFY-B |
MSDS | |
Size | Pls inquire |
Source | E.coli |
Conjugate | Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag. |
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Code | CSB-BP352404IFY |
MSDS | |
Size | Pls inquire |
Source | Baculovirus |
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Code | CSB-MP352404IFY |
MSDS | |
Size | Pls inquire |
Source | Mammalian cell |
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This Recombinant influenza A virus Matrix protein 1 (M1) is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered.
The Influenza A virus Matrix protein 1 (M1) is a crucial protein involved in various stages of the influenza virus life cycle, including viral replication, assembly, and budding [1]. It plays a significant role in regulating the transport of viral ribonucleoproteins into and out of the nucleus [2]. Additionally, M1 is essential for maintaining the integrity and shape of the virus, organizing the virus membrane, and forming a continuous matrix layer underneath the viral envelope [3]. The M1 protein Y132 phosphorylation is crucial for regulating its nuclear import and virus replication [4]. Evidence has shown that the M1 protein is helpful for the recognition of infected cells by cytotoxic T cells [5].
References:
[1] S. Cao, X. Liu, M. Yu, J. Li, X. Jia, Y. Biet al., A nuclear export signal in the matrix protein of influenza a virus is required for efficient virus replication, Journal of Virology, vol. 86, no. 9, p. 4883-4891, 2012. https://doi.org/10.1128/jvi.06586-11
[2] G. Whittaker, I. Kemler, & A. Helenius, Hyperphosphorylation of mutant influenza virus matrix protein, m1, causes its retention in the nucleus, Journal of Virology, vol. 69, no. 1, p. 439-445, 1995. https://doi.org/10.1128/jvi.69.1.439-445.1995
[3] W. Zhang, W. Zheng, Y. Toh, M. Betancourt-Solis, J. Tu, Y. Fanet al., Crystal structure of an orthomyxovirus matrix protein reveals mechanisms for self-polymerization and membrane association, Proceedings of the National Academy of Sciences, vol. 114, no. 32, p. 8550-8555, 2017. https://doi.org/10.1073/pnas.1701747114
[4] S. Wang, Z. Zhao, Y. Bi, L. Sun, X. Liu, & W. Liu, Tyrosine 132 phosphorylation of influenza a virus m1 protein is crucial for virus replication by controlling the nuclear import of m1, Journal of Virology, vol. 87, no. 11, p. 6182-6191, 2013. https://doi.org/10.1128/jvi.03024-12
[5] T. Braciale, Immunologic recognition of influenza virus-infected cells. ii. expression of influenza a matrix protein on the infected cell surface and its role in recognition by cross-reactive cytotoxic t cells, The Journal of Experimental Medicine, vol. 146, no. 3, p. 673-689, 1977. https://doi.org/10.1084/jem.146.3.673
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