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Di-Methyl-RPL29 (Lys5) (D8T9P) Rabbit Monoclonal Antibody #19495
Filter:
- WB
Product Specifications
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 23 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
实验步骤
Specificity / Sensitivity
Di-Methyl-RPL29 (Lys5) (D8T9P) Rabbit Monoclonal Antibody recognizes endogenous levels of RPL29 protein only when methylated at Lys5. This antibody shows slight cross-reactivity to mono-methyl-RPL29 Lys5.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic methyl peptide corresponding to residues surrounding Lys5 of human RPL29 protein.
Background
SET7/SET9 is a member of the SET domain-containing family, and can specifically methylate Lys4 on histone H3 (1). Like most other lysine-directed histone methyltransferases, it contains a conserved catalytic SET domain originally identified in the Drosophila Su(var)3-9, Enhancer of zeste and Trithorax proteins. Histone methylation is a major determinant for the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (2,3). Methylation of histone H3 Lys4 enhances transcriptional activation by coordinating the recruitment of BPTF, a component of the NURF chromatin remodeling complex, and WDR5, a component of multiple histone methyltransferase complexes (4,5). In addition, methylation of lysine 4 blocks transcriptional repression by inhibiting the binding of the NURD histone deacetylation complex to the amino-terminal tail of histone H3 and interfering with SUV39H1-mediated methylation of histone H3 Lys9 (1). SET7/SET9 is highly active on free histone H3, but only very weakly methylates H3 within nucleosomes (1). Besides histones, SET7/SET9 also methylates Lys189 of the TAF10, a member of the TFIID transcription factor complex, and Lys372 of the p53 tumor suppressor protein (6,7). Methylation of TAF10 stimulates transcription in a promoter-specific manner by increasing the affinity of TAF10 for RNA polymerase II, which may potentiate pre-initiation complex formation (6). Methylation of p53 at Lys372 increases protein stability and leads to upregulation of target genes such as p21. Thus the loss of SET7/SET9 may represent another mechanism for the inactivation of p53 in human cancers (7).
Ribosomal protein L29 (RPL29) is a ubiquitously expressed protein subunit of the cytoplasmic eukaryotic large 60S ribosomal subunit that functions in the translation of RNA to protein. RPL29 is a non-histone substrate of the SET7/SET9 protein methyltransferase and is exclusively mono- and di-methylated on lysine 5 by SET7/SET9. In addition, RPL29 lysine 5 is demethylated by the LSD1 protein demethylase (8). This antibody provides a specific readout for SET7/SET9 methyltransferase and LSD1 demethylase activities.
Ribosomal protein L29 (RPL29) is a ubiquitously expressed protein subunit of the cytoplasmic eukaryotic large 60S ribosomal subunit that functions in the translation of RNA to protein. RPL29 is a non-histone substrate of the SET7/SET9 protein methyltransferase and is exclusively mono- and di-methylated on lysine 5 by SET7/SET9. In addition, RPL29 lysine 5 is demethylated by the LSD1 protein demethylase (8). This antibody provides a specific readout for SET7/SET9 methyltransferase and LSD1 demethylase activities.
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- Kubicek, S. et al. (2006) Ernst Schering Res. Found. Workshop , 1-27.
- Lin, W. and Dent, S.Y. (2006) Curr. Opin. Genet. Dev. 16, 137-142.
- Wysocka, J. et al. (2006) Nature 442, 86-90.
- Wysocka, J. et al. (2005) Cell 121, 859-872.
- Kouskouti, A. et al. (2004) Mol. Cell 14, 175-182.
- Chuikov, S. et al. (2004) Nature 432, 353-360.
- Hamidi, T. et al. (2018) J Biol Chem , .
Alternate Names
60S ribosomal protein L29; Cell surface heparin-binding protein HIP; heparin/heparan sulfate-binding protein; heparin/heparan sulfate-interacting protein; HIP; HP/HS-interacting protein; HUMRPL29; L29; Large ribosomal subunit protein eL29; MGC88589; ribosomal protein L29; ribosomal protein YL43 homologue; RL29; RPL29; RPL29_3_370; RPL29P10
限制使用
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For Research Use Only. Not for Use in Diagnostic Procedures.
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