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Methylated (ε-N) Lysine Antibody

Catalog # Pack Size Price(USD)
ICP0501 100 µg $350.00


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
250 µg/mL in Tris-phosphate buffer, 50% glycerol
Methylated KLH conjugates
The antibody was immunoaffinity purified with epsilon N-methyl lysine on agarose.
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.
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

       2J. Biol. Chem. 2002. 277: 34655-34657. doi:10.1074/jbc.C200433200

       3. J. Biol. Chem. 2002. 277: 11621-11624. doi:10.1074/jbc.C200045200

        4Biochem & 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