MLL1 (E9W9Z) Rabbit mAb (Carboxy-terminal Antigen) #34907
- WB
- IP
- ChIP
Supporting Data
| REACTIVITY | H Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 180 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- ChIP-Chromatin Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
| Chromatin IP | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Background
MLL1 functions as a master regulator of both embryogenesis and hematopoiesis, and is required for proper expression of Hox genes (7,8). MLL1 is a large, approximately 4000 amino acid, protein that is cleaved by the taspase 1 threonine endopeptidase to form N-terminal (MLL1-N) and C-terminal MLL1 (MLL1-C) fragments, both of which are subunits of the functional MLL1/COMPASS complex (9,10). MLL1-N, MLL1-C, WDR5, RBBP5 and ASH2L define the core catalytic component of the MLL1/COMPASS complex, which is recruited to target genes and methylates histone H3 lysine 4 to regulate transcriptional initiation (11). At least 60 different MLL1 translocation partners have been molecularly characterized and associated with various hematological malignancies. The most common translocation partners include AF4, AF9, ENL, AF10, ELL and AF6 (8,12,13). With the exception of AF6, all of these partners are nuclear proteins that function to positively regulate transcriptional elongation. AF4, AF9 and ENL are all components of the super elongation complex (SEC), while AF4, AF9, AF10 and ENL all interact with the histone H3 lysine 79 methyltransferase DOT1L. Many MLL1 target genes are normally regulated by promoter-proximal pausing, with the release of RNA polymerase and transcriptional elongation occurring in response to proper stimuli (14). The association of MLL1 translocation partners with SEC and DOT1L suggest that MLL1-fusion proteins may function to sustain specific gene expression programs by constitutively activating transcriptional elongation.
- Miller, T. et al. (2001) Proc Natl Acad Sci U S A 98, 12902-7.
- Shilatifard, A. (2008) Curr Opin Cell Biol 20, 341-8.
- Tenney, K. and Shilatifard, A. (2005) J Cell Biochem 95, 429-36.
- Lee, J.H. and Skalnik, D.G. (2005) J Biol Chem 280, 41725-31.
- Lee, J.H. et al. (2007) J Biol Chem 282, 13419-28.
- Hughes, C.M. et al. (2004) Mol Cell 13, 587-97.
- Eissenberg, J.C. and Shilatifard, A. (2010) Dev Biol 339, 240-9.
- Smith, E. et al. (2011) Genes Dev 25, 661-72.
- Takeda, S. et al. (2006) Genes Dev 20, 2397-409.
- Yokoyama, A. et al. (2002) Blood 100, 3710-8.
- Dou, Y. et al. (2006) Nat Struct Mol Biol 13, 713-9.
- Yip, B.H. and So, C.W. (2013) Exp Biol Med (Maywood) 238, 315-23.
- Neff, T. and Armstrong, S.A. (2013) Blood 121, 4847-53.
- Wang, P. et al. (2009) Mol Cell Biol 29, 6074-85.
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