|Application ||WB, IF, E|
|Calculated MW||36949 Da|
|Other Names||Polycomb complex protein BMI-1, Polycomb group RING finger protein 4, RING finger protein 51, BMI1, PCGF4, RNF51|
|Target/Specificity||This BMI1 monoclonal antibody is generated from mouse immunized with BMI1 recombinant protein.|
|Format||Purified monoclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||BMI1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:15386022, PubMed:16359901, PubMed:26151332, PubMed:16714294, PubMed:21772249, PubMed:25355358, PubMed:27827373). The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A (PubMed:21772249, PubMed:25355358). In the PRC1-like complex, regulates the E3 ubiquitin-protein ligase activity of RNF2/RING2 (PubMed:15386022, PubMed:26151332, PubMed:21772249).|
|Cellular Location||Nucleus. Cytoplasm|
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Component of the Polycomb group (PcG) multiprotein PRC1 complex, a complex required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. In the PRC1 complex, it is required to stimulate the E3 ubiquitin-protein ligase activity of RNF2/RING2.
Ismail, I.H., et al. J. Cell Biol. 191(1):45-60(2010)
Yang, M.H., et al. Nat. Cell Biol. 12(10):982-992(2010)
Kikuchi, J., et al. Cancer 116(12):3015-3024(2010)
Honig, A., et al. Anticancer Res. 30(5):1559-1564(2010)
Venkataraman, S., et al. PLoS ONE 5 (6), E10748 (2010) :
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