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Anti-Methyl (mono-, di-) Lysine, HRP conjugate (ICP0502) |
| Catalog Number |
Pack Size |
Price (US) |
| ICP0502-100 |
100µg |
$350 |
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Description: Affinity purified rabbit polyclonal anti-methylated lysine antibodies are developed using a unique technique of ImmuneChem. The methylated lysine antibodies are affinity purified using N-methyl (epsilon amino group) lysine on agarose as affinity matrix. The purified antibody was conjugated to horse radish peroxidase (HRP) via reductive amination. Direct label of primary anti-MeK will avoid the use of secondary antibodies therefore eliminating the interference of the 2nd antibody-conjugates. The antibodies could be utilized for detection, quantitation and isolation of proteins with MeK residues. |
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Species: Rabbit
Formulation: 250 µg/mL in PBS, pH 7.0, 50% glycerol
Storage & Stability: Store product at –20 0C. One year from date of shipping
Immunogen: Methylated KLH conjugates
Purification: Methyl-lysine and di-methyl-lysine on agarose
Specificity: MeK, perixidase conjugate recognizes proteins methylated on lysine residues (mono and di-methylysine). It does not cross-react with acetylated proteins.
Conjugation: reductive amination, HRP/Ab molar ratio: 2:1
Western blot : Western blot analysis of the methylated protein pattern in whole Hela cell with ICP0502
A: Signal of methylated proteins
B: Signal of the methylated proteins was competitively suppressed by 50 ug/mL of methylated BSA.
C: Signal of the methylated proteins was competitively suppressed by 10 ug/mL of methylated BSA
Application(s): ELISA, WB.
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, 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]
References: 1. Im, H. et al. J. Biol. Chem. 2003, 278, 18346-18352.
2. Ng, H. H. et al. J. Biol. Chem. 2002, 277, 34655-34657.
3. Zegerman, P. et al. J. Biol. Chem. 2002, 277, 11621-11624.
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