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Methylated (ε-N) Lysine Antibody
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Product Description
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The affinity purified rabbit polyclonal anti-methylated lysine antibody was developed using a technique unique to ImmuneChem. The methylated lysine antibodies are affinity purified using N-methyl (epsilon amino group) lysine on agarose as the affinity matrix. The antibodies could be utilized for detection, quantization and isolation of proteins with methylated lysine residues.
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 Western blot analysis of the methylated histone from melanoma cells with anti-methylated lysine anti-MeK (ICP0501). Histones were isolated with cold 0.1M HCl extraction followed by:
A: Blot with 0.5 µg/mL of anti-MeK (ICP0501) in TBSt and blocked with synthetic methylated BSA 100 µg/mL
B: Blot with 0.5 µg/mL of anti-MeK (ICP0501) in TBSt
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Species
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Rabbit
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Formulation
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250 µg/mL in Tris-phosphate buffer, 50% glycerol
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Immunogen
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Methylated KLH conjugates
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Purification
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The antibody was immunoaffinity purified with epsilon N-methyl lysine on agarose.
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Specificity
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The antibody recognizes proteins or peptides methylated on lysine residues (mono, di-methyllysine). There are no cross reactions with acetylated proteins. The cross reactivity with tri-methyl lysine has not been tested.
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Applications
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ELISA; WB; IHC
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Scientific Description
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MeK is a conserved post-translational modification and is an important biochemical process for many protein-protein interactions. It is found in many proteins, for example calmodulin, cytochrome C, chromosomal proteins, histones and non-histones as well as neural storage body proteins. It has been suggested that methylation of lysine plays an important role in gene silencing. [1-3]
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Storage & Stability
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Store product at -20°C. Expiration date is one year from date of shipping if stored properly.
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Product Specific References
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1. J. Biol. Chem. 2003. 278: 18346-18352. doi.10.1074/jbc.M300890200 2. J. Biol. Chem. 2002. 277: 34655-34657. doi:10.1074/jbc.C200433200 3. J. Biol. Chem. 2002. 277: 11621-11624. doi:10.1074/jbc.C200045200 4. Biochem & Biophys Res. Com. 2014. 451 (2): 229-234. doi:10.1016/j.bbrc.2014.07.11 5. Mol. BioSyst. 2013. 9: 2231-2247. doi: 10.1039/C3MB00009E 6. Biochemical and Biophysical Research Communications Volume 451, Issue 2, 22 August 2014, Pages 229–234. doi: 10.1016/j.bbrc.2014.07.110. 7. Proteomics. 2015. 15 (13): 2166–2176. doi: 10.1002/pmic.201400521 8. BioRxiv 2018. doi: 10.1101/240952 9. The FEBS Journal 2019. doi: 10.1111/febs.14867 10. EMBO Reports. 2019. 20(5): e43260. doi: 10.15252/embr.201643260 11. Nature Communications. 2018. 9(1):3436. doi: 10.1038/s41467-018-05451-7
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