抗Methylated Lysineポリクローナル抗体(Anti-Methylated Lysine) Methylated Lysine antibody | StressMarq Biosciences

Western blot analysis of Methylated Lysine in BSA (Left) and Methylated BSA (Right), using a 1:1000 dilution of SPC-158.

Methylated Lysine Antibody

Polyclonal

Anti-Methylated Lysine

Cell Signaling, Post-translational Modifications

dimethylysine, methyl lysine, N epsilon dimethyl lysine, trimethyl lysine

N/A

Rabbit

N/A

Methylated KLH Conjugated

WB, IP, ELISA, IHC, Dot Blot

Multi species

N/A

N/A

Detects proteins containing methylated lysine residues. There is no cross-reaction with acetylated lysine. Cross-reactivity with tri-methyllysine has not yet been tested.

1:2000-1:5000 (WB)

Affinity Purified

PBS, 50% glycerol, 0.09% sodium azide

0.2-0.5 µg/mL of SPC-158 was sufficient for detection of the methylated histone by western blot analysis using melanoma cells in TBSt.

Research Background
Post-translational modifications of proteins play critical roles in the regulation and function of many known biological processes. Proteins can be post-translationally modified in many different ways, and a common post-transcriptional modification of Lysine involves methylation (1). Lysine can be methylated once, twice or three times by lysine methyltransferases. The transfer of methyl groups from S-adenosyl methionine to histones is catalyzed by enzymes known as histone methyltransferases. Histones which are methylated on certain residues can act epigenetically to repress or activate gene expression (1, 2). The transcriptional repressor SUV39H1 can encode novel enzymes which selectively methylate histone H3 at lysine 9. SUV39H1 places a methyl marker on histone H3, which is then recognized by HP1 through its chromo domain. This model may also explain the stable inheritance of the heterochromatic state (3). Some studies have also speculated a stimulatory role for transcription by methylated histone lyside 4 due to its presence at active transcription sites (4-6).

References
1. Yang XJ. (2005). Oncogene. 24:1653-1662.

2. Melcher M. et al. (2000). Mol Cell Biol 20: 3728– 3741.

3. Bannister AJ. et al. (2001). Nature 410(6824): 120-4.

4. Im H. et al. (2003). J Biol Chem. 278: 18346-18352.

5. Ng H.H., et al. (2002). J Biol Chem. 277: 34655-34657.

6. Zegerman P., et al. (2002). J Biol Chem. 277: 11621- 11624.

Cited References
1.  Dawson, N.J., Bell, R.A.V. and Storey, K.B. (2013). Purification and Properties of White Muscle Lactate Dehydrogenase from the Anoxia-Tolerant Turtle, the Red-Eared Slider, Trachemys scripta elegans. 2013. Article ID 784973. 

2. Shahriaria A., Dawsonb N., Bellb R., Storey, K. (2013). Stable suppression of lactate dehydrogenase activity during anoxia in the foot muscle of Littorinalittorea and the potential role of acetylation as a novel posttranslational regulatory mechanism. University of Ahvaz, Ahvaz, Iran, Carleton University, Ottawa, Canada. Link to

3. Katzenback, B.A., Dawson, N.J., Storey, K.B. (2014). Purification and characterization of a urea sensitive lactate dehydrogenase from the liver of the African clawed frog, Xenopus laevis. J Comp Physiol B.