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Product Description | 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. |  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 | |
Species | Rabbit | ||
Formulation | 250 µg/mL in Tris-phosphate buffer, 50% glycerol | ||
Immunogen | Methylated KLH conjugates | ||
Purification | The antibody was immunoaffinity purified with epsilon N-methyl lysine on agarose. | ||
Specificity | 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. | ||
Applications | ELISA; WB; IHC | ||
Scientific Description | 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] | ||
Storage & Stability | Store product at -20°C. Expiration date is one year from date of shipping if stored properly. | ||
Product Specific References | 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. BioRxiv2018. 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
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