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

•        doi.10.1074/jbc.M300890200
•        . J. Biol. Chem. 2002. 277: 34655-34657.doi:10.1074/jbc.C200433200
•        . J. Biol. Chem. 2002. 277: 11621-11624.doi:10.1074/jbc.C200045200

        . Biochem & Biophys Res. Com. 2014. 451 (2): 229-234.    doi:10.1016/j.bbrc.2014.07.11

        doi: 10.1039/C3MB00009E

       . Proteomics.doi: 10.1002/pmic.201400521