| References |
| Formulation |
400 µl (0.25 mg/ml) of affinity-purified IgG in PBS containing 50% glycerol |
| Stability |
1 year |
| Storage |
-20°C |
| Shipping |
Wet ice
in continental US; may vary elsewhere
|
| Specificity |
| Methylated lysine residues |
+ |
|
Background Reading
Im, H., Park, C., Feng, Q., et al. Dynamic regulation of histone H3 methylated at lysine 79 within a tissue-specific chromatin domain. J Biol Chem 278(20) 18346-18352 (2003).
Yang, X. Multisite protein modification and intramolecular signaling. Oncogene 24 1653-1662 (2005).
Melcher, M., Schmid, M., Aagaard, L., et al. Structure-function analysis of SUV39H1 reveals a dominant role in heterochromatin organization, chromosome segregation, and mitotic progression. Mol Cell Biol 20(10) 3728-3841 (2000).
| Size |
Global Purchasing |
| 400 µL |
|
Description
Antigen:
methylated KLH
·
Host:
rabbit
·
Application(s):
WB and ELISA
·
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
1
Yang, X. Multisite protein modification and intramolecular signaling. Oncogene 24 1653-1662 (2005).
2
Melcher, M., Schmid, M., Aagaard, L., et al. Structure-function analysis of SUV39H1 reveals a dominant role in heterochromatin organization, chromosome segregation, and mitotic progression. Mol Cell Biol 20(10) 3728-3841 (2000).
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