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Catalog # Product Description |
ICP0601 This rabbit polyclonal antibody is specifically isolated and affinity purified from the anti-serum using chemically methylated protein antigen. The affinity purified trimethylated lysine antibodies are affinity absorbed with N-(epsilon) mono- and di-methylated lysine. The antibodies could be utilized for detection and quantization of proteins with N-trimethylated lysine residues. |
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Immunohistochemistry of the human tissue with ICP0601
Western blot analysis of protein trimethylated from human melanoma cell (MMRU) with ICP0601. A. Primary antibody B. Primary antibody plus 50mg/mL of methylated protein BSA (ICP0504)
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Species
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Rabbit
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Formulation
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250 μg/mL in PBS, 50% glycerol
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Immunogen
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Methylated KLH conjugates
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Purification
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N-(epsilon) trimethyllysine on agarose and immunoaffinity absorbed with N-(epsilon) methylated lysine and N-(epsilon) dimethylated lysine on agarose
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Specificity
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Recognizes proteins with trimethylation on lysine residues (N-epsilon); antibody does not cross react with acetylated proteins or mono- and dimethylated proteins.
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Species Tested
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Human, rat, mouse, bovine and pig
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Applications
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ELISA (1:2000); WB (1:2000); IP (5 μg/mg protein sample); IF (5 μg/mL or 1:100)
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Scientific Description
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In the biosynthetic pathway of 1-carnitine, epsilon-N-trimethyllysine hydroxylase is the first enzyme that catalyzes the formation of beta-hydroxy-N-epsilon-trimethyllysine from epsilon-N-trimethyllysine. This reaction is dependent on alpha ketoglutarate, Fe2+, and oxygen.
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Storage & Stability
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Product is stable for several weeks at 4°C. For extended storage, store product at -20°C. Expiration date is three years from date of shipping if stored properly.
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Product Specific References |
1. J. Bacteriol. 2012. 194 (23): 6410-6418. 2. J Biol Chem. 2001. 36 (276): 33512-33517. 3. Biochem. Biophys. Res. Commun. 2014. 451 (2): 229-234. 4. Proteomics. 2015. 15 (13): 2166-2176. doi: 10.1002/pmic.201400521 5. Mol. BioSyst. 2013. 9: 2231-2247. doi: 10.1039/C3MB00009E 6. Sci Rep. 2016. 6: 35432. 1-24. doi: 10.1038/srep35432 |
