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Methylated Lysine Antibody, HRP
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Catalog# Product Description |
ICP0502 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 purified antibody was conjugated to horse radish peroxidase (HRP) via reductive amination. Direct labelling of primary anti-MeK will avoid the use of secondary antibodies therefore eliminating the interference of the secondary antibody-conjugates. The antibodies could be utilized for detection, quantization and isolation of proteins with MeK residues. |
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Western blot analysis of the methylated protein pattern in whole HeLa cells with ICP0502.
A. Signal of methylated proteins
B. Signal of the methylated proteins was competitively suppressed by 50 µg/mL of methylated BSA
C. Signal of the methylated proteins was competitively suppressed by 10 µg/mL of methylated BSA
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Species
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Rabbit
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Formulation
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500 µg/mL in HRP stabilizing buffer with 50% glycerol
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Immunogen
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Methylated KLH conjugates
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Purification
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Methyl-lysine and di-methyl lysine on agarose
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Conjugation
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Reductive amination; HRP/Ab molar ratio - 10:1
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Specificity
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Anti-MeK peroxidase conjugates recognize proteins methylated on their lysine residues (mono and di-methyllysine). They do not cross react with acetylated proteins.
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Applications
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ELISA; WB
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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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Product is stable for several weeks at 4°C. For extended storage, store product at -20°C. Expiration date is six months 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 |
