SET1/COMPASS Antibody Sampler Kit #25501
Product Information
Kit Usage Information
Protocols
- 6891: Western Blotting, Immunofluorescence
- 7074: Western Blotting
- 13105: Western Blotting, ChIP Magnetic, Chromatin IP-seq, CUT&RUN Assay
- 14197: Western Blotting, Immunoprecipitation (Agarose), Immunofluorescence*
- 14689: Western Blotting, Immunoprecipitation (Magnetic), CUT&RUN Assay, CUT&Tag
- 44922: Western Blotting, Immunoprecipitation (Agarose)
- 61702: Western Blotting, Immunoprecipitation (Magnetic), ChIP Magnetic, Chromatin IP-seq, CUT&RUN Assay, CUT&Tag
- 63735: Western Blotting, Immunoprecipitation (Magnetic), Immunofluorescence, CUT&RUN Assay
- 99715: Western Blotting, Immunoprecipitation (Magnetic)
Product Description
Specificity / Sensitivity
Source / Purification
Background
Like yeast Set1, all six Set1-related mammalian proteins methylate histone H3 on lysine 4 (2-6). SET1A, SET1B, MLL1 and MLL2 mediate di- and tri-methylation of histone H3 Lys4 at gene promoters to facilitate transcription activation. MLL3 and MLL4 function primarily to mono-methylate histone H3 Lys4 at gene enhancers. MLL1 and MLL2 function as master regulators of both embryogenesis and hematopoiesis, and are required for proper expression of Hox genes (8-10). 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 (11,12). MLL1 translocations are found in a large number of hematological malignancies, suggesting that Set1 histone methyltransferase complexes play a critical role in leukemogenesis (6). Like MLL1, MLL2 is also a large, approximately 2700 amino acid protein that is cleaved by the Taspase 1 threonine endopeptidase to form N-terminal (MLL2-N) and C-terminal (MLL2-C) fragments, both of which are subunits of the functional MLL2/COMPASS complex. MLL2 has also been implicated as a modulator of hematological malignancies (13). MLL3 and MLL4 proteins are not cleaved by Taspase 1.
- 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.
- Yokoyama, A. et al. (2004) Mol Cell Biol 24, 5639-49.
- Eissenberg, J.C. and Shilatifard, A. (2010) Dev Biol 339, 240-9.
- Smith, E. et al. (2011) Genes Dev 25, 661-72.
- Denissov, S. et al. (2014) Development 141, 526-37.
- Takeda, S. et al. (2006) Genes Dev 20, 2397-409.
- Yokoyama, A. et al. (2002) Blood 100, 3710-8.
- Chen, Y. et al. (2017) Cancer Cell 31, 755-770.e6.
Limited Uses
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