Code | CSB-YP676104ENV |
MSDS | |
Size | Pls inquire |
Source | Yeast |
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Code | CSB-EP676104ENV |
MSDS | |
Size | Pls inquire |
Source | E.coli |
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Code | CSB-EP676104ENV-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-BP676104ENV |
MSDS | |
Size | Pls inquire |
Source | Baculovirus |
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Code | CSB-MP676104ENV |
MSDS | |
Size | Pls inquire |
Source | Mammalian cell |
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Protein/nucleic acid deglycase 3 (YajL) is a multifunctional protein involved in various cellular processes. YajL has been identified as a deglycase that repairs methylglyoxal (MGO)-damaged proteins [1]. Additionally, it has been shown to protect cells against protein sulfenylation, suggesting its function as a covalent chaperone dedicated to the detection of sulfenylated proteins [2]. YajL also exhibits chaperone activity, protecting bacteria against oxidative stress-induced protein aggregation and controlling gene expression [3][4]. The crystal structures of YajL and DJ-1, a Parkinsonism-associated protein, are strikingly similar, indicating that they may share similar functions [5]. Furthermore, YajL is prone to oxidation at a specific residue and requires this residue to confer protection against hydrogen peroxide stress in E. coli, suggesting similarities in function with human DJ-1 [6]. The structural correspondence between YajL and DJ-1 is so close that their backbone structures are essentially identical [7]. Moreover, YajL, as a member of the DJ-1/Hsp31/PfpI superfamily, functions as a covalent chaperone involved in the detection of sulfenylated proteins by forming mixed disulfide bonds with them [8].
References:
[1] S. Qaidi, N. Scott, & P. Hardwidge, "Arginine glycosylation enhances methylglyoxal detoxification", Scientific Reports, vol. 11, no. 1, 2021. https://doi.org/10.1038/s41598-021-83437-0
[2] V. Gautier, H. Le, A. Malki, N. Messaoudi, T. Caldas, F. Kthiriet al., "Yajl, the prokaryotic homolog of the parkinsonism-associated protein dj-1, protects cells against protein sulfenylation", Journal of Molecular Biology, vol. 421, no. 4-5, p. 662-670, 2012. https://doi.org/10.1016/j.jmb.2012.01.047
[3] H. Le, V. Gautier, F. Kthiri, A. Malki, N. Messaoudi, M. Mihoubet al., "Yajl, prokaryotic homolog of parkinsonism-associated protein dj-1, functions as a covalent chaperone for thiol proteome", Journal of Biological Chemistry, vol. 287, no. 8, p. 5861-5870, 2012. https://doi.org/10.1074/jbc.m111.299198
[4] S. Burschel, D. Decovic, F. Nuber, M. Stiller, M. Hofmann, A. Zupoket al., "Iron‐sulfur cluster carrier proteins involved in the assembly of escherichia coli nadh:ubiquinone oxidoreductase (complex i)", Molecular Microbiology, vol. 111, no. 1, p. 31-45, 2018. https://doi.org/10.1111/mmi.14137
[5] N. Messaoudi, V. Gautier, F. Kthiri, G. Lelandais, M. Mihoub, D. Joseleau-Petitet al., "Global stress response in a prokaryotic model of dj-1-associated parkinsonism", Journal of Bacteriology, vol. 195, no. 6, p. 1167-1178, 2013. https://doi.org/10.1128/jb.02202-12
[6] M. Wilson, "The role of cysteine oxidation in dj-1 function and dysfunction", Antioxidants & Redox Signaling, vol. 15, no. 1, p. 111-122, 2011. https://doi.org/10.1089/ars.2010.3481
[7] M. Wilson, D. Ringe, & G. Petsko, "The atomic resolution crystal structure of the yajl (thij) protein from escherichia coli: a close prokaryotic homologue of the parkinsonism-associated protein dj-1", Journal of Molecular Biology, vol. 353, no. 3, p. 678-691, 2005. https://doi.org/10.1016/j.jmb.2005.08.033
[8] Y. Saito, "Oxidized dj-1 as a possible biomarker of parkinson’s disease", Journal of Clinical Biochemistry and Nutrition, vol. 54, no. 3, p. 138-144, 2014. https://doi.org/10.3164/jcbn.13-108
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KEGG: ecj:JW5057
STRING: 316385.ECDH10B_0380