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Methylated Lysine (meLys) antibody (Biotin)
Alternatives Western Blotting (WB), ELISA, Immunoprecipitation (IP)
|6 references available|
|Price||412.50 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 3 to 4 Business Days|
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. 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. 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. Some studies have also speculated a stimulatory role for transcription by methylated histone lyside 4 due to its presence at active transcription sites.
Synonyms: dimethylysine, methyl lysine, N epsilon dimethyl lysine, trimethyl lysine
|Specificity||Detects proteins containing methylated lysine residues in SDS PAGE immunoblots.|
|Application Notes||1:2000-1:5000 dilution WB|
|Buffer||PBS, 50% glycerol|
|Preservative||0.09% sodium azide|
|Storage||Store at -20° C. Shipping Temperature: Blue Ice or 4° C|
|Storage Shipping Temp Max||Blue Ice or 4 °C|
|Research Area||Cell Signaling, Metabolism|
|Restrictions||For Research Use only|
Melcher, Schmid, Aagaard et al.: "Structure-function analysis of SUV39H1 reveals a dominant role in heterochromatin organization, chromosome segregation, and mitotic progression." in: Molecular and cellular biology, Vol. 20, Issue 10, pp. 3728-41, 2000 (PubMed).
Bannister, Zegerman, Partridge et al.: "Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain." in: Nature, Vol. 410, Issue 6824, pp. 120-4, 2001 (PubMed).
Zegerman, Canas, Pappin et al.: "Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex." in: The Journal of biological chemistry, Vol. 277, Issue 14, pp. 11621-4, 2002 (PubMed).
Ng, Xu, Zhang et al.: "Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79." in: The Journal of biological chemistry, Vol. 277, Issue 38, pp. 34655-7, 2002 (PubMed).
Im, Park, Feng et al.: "Dynamic regulation of histone H3 methylated at lysine 79 within a tissue-specific chromatin domain." in: The Journal of biological chemistry, Vol. 278, Issue 20, pp. 18346-52, 2003 (PubMed).
Yang: "Multisite protein modification and intramolecular signaling." in: Oncogene, Vol. 24, Issue 10, pp. 1653-62, 2005 (PubMed).
|Reactivities||All Species (2)|
|Applications||ELISA (12), Western Blotting (WB) (12), Immunoprecipitation (IP) (6), Immunohistochemistry (Frozen Sections) (IHC (fro)) (1), Immunohistochemistry (IHC) (1)|
|Conjugates||HRP (4), Biotin (3)|