|Other Names||Histone-lysine N-methyltransferase 2A, Lysine N-methyltransferase 2A, ALL-1, CXXC-type zinc finger protein 7, Myeloid/lymphoid or mixed-lineage leukemia, Myeloid/lymphoid or mixed-lineage leukemia protein 1, Trithorax-like protein, Zinc finger protein HRX, MLL cleavage product N320, N-terminal cleavage product of 320 kDa, p320, MLL cleavage product C180, C-terminal cleavage product of 180 kDa, p180, KMT2A, ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6182a was selected from the C-term region of human MLL1 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1|
|Function||Histone methyltransferase that plays an essential role in early development and hematopoiesis. Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac). In the MLL1/MLL complex, it specifically mediates H3K4me, a specific tag for epigenetic transcriptional activation (PubMed:12453419, PubMed:20677832, PubMed:26886794). Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity (PubMed:19187761, PubMed:26886794). Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9'. Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state (PubMed:20010842). Required for transcriptional activation of HOXA9 (PubMed:12453419, PubMed:20677832, PubMed:20010842). Promotes PPP1R15A-induced apoptosis. Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-ARNTL/BMAL1 heterodimer. Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-ARNTL/BMAL1 to chromatin (By similarity).|
|Cellular Location||Nucleus. MLL cleavage product C180: Nucleus. Note=Localizes to a diffuse nuclear pattern when not associated with MLL cleavage product N320|
|Tissue Location||Heart, lung, brain and T- and B-lymphocytes.|
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Chromosome 11q23 translocations targeting mixed-lineage leukemia 1 (MLL) gene have been correlated with human acute leukemias, including lymphoid, myeloid, monoblastic and myelomonocytic varieties. More than 3 dozen genes that fuse to with MLL have been identified in various types of malignancies, including AF4, AF9, ENL, CBL, LARG, LPP, GMPS, and FBP17. The 431 kDa MLL protein exhibits greatest abundancy in cerebral cortex, kidney, thyroid, and lymphoid tissues. Inside the cell, MLL is part of a stable multiprotein supercomplex, the majority of which are components of transcription complexes, including TFIID. The MLL multiprotein complex seems to remodel, acetylate, deacetylate, and methylate nucleosomes and/or free histones. MLL contains a SET domain characteristic for histone H3 lysine-4-specific methyltransferases. Oncogenic MLL fusion proteins appear to alter the methyltransferase activity of wild-type MLL.
Bertrand, F.E., et al., Leukemia 17(12):2454-2459 (2003).Dyson, M.J., et al., Cancer Genet. Cytogenet. 147(1):81-83 (2003).Xia, Z.B., et al., Proc. Natl. Acad. Sci. U.S.A. 100(14):8342-8347 (2003).Ferrando, A.A., et al., Blood 102(1):262-268 (2003).Echlin-Bell, D.R., et al., Hum. Genet. 113(1):80-91 (2003).
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